HOMCOS(prot_sch_conbars.cgi):

		Contact Molecules for Homologous Proteins
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PID

QueryLength

Homolgous Sequence in PDB

UniProt Query

TITLE

1687785

7096

500

P0DTD1(R1AB_SARS2)

RecName: Full=Replicase polyprotein 1ab; Short=pp1ab;AltName: Full=ORF1ab polyprotein;Contains: RecName: Full=Host translation inhibitor nsp1; AltName: Full=Leader protein; AltName: Full=Non-structural protein 1; Short=nsp1;Contains: RecName: Full=Non-structural protein 2; Short=nsp2; AltName: Full=p65 homolog;Contains: RecName: Full=Papain-like protease nsp3 ; EC=3.4.19.12 ; EC=3.4.22.-; AltName: Full=Non-structural protein 3; Short=nsp3; AltName: Full=PL2-PRO; AltName: Full=Papain-like proteinase; Short=PL-PRO;Contains: RecName: Full=Non-structural protein 4; Short=nsp4;Contains: RecName: Full=3C-like proteinase nsp5; Short=3CL-PRO; Short=3CLp; EC=3.4.22.69 ; AltName: Full=Main protease; Short=Mpro ; AltName: Full=Non-structural protein 5; Short=nsp5; AltName: Full=SARS coronavirus main proteinase;Contains: RecName: Full=Non-structural protein 6; Short=nsp6;Contains: RecName: Full=Non-structural protein 7; Short=nsp7;Contains: RecName: Full=Non-structural protein 8; Short=nsp8;Contains: RecName: Full=RNA-capping enzyme subunit nsp9; AltName: Full=Non-structural protein 9; Short=nsp9; EC=2.7.7.50 ;Contains: RecName: Full=Non-structural protein 10; Short=nsp10; AltName: Full=Growth factor-like peptide; Short=GFL;Contains: RecName: Full=RNA-directed RNA polymerase nsp12; Short=Pol; Short=RdRp; EC=2.7.7.48; AltName: Full=Non-structural protein 12; Short=nsp12;Contains: RecName: Full=Helicase nsp13; Short=Hel; EC=3.6.4.12; EC=3.6.4.13; AltName: Full=Non-structural protein 13; Short=nsp13;Contains: RecName: Full=Guanine-N7 methyltransferase nsp14; EC=2.1.1.56 ; EC=3.1.13.-; AltName: Full=Non-structural protein 14; Short=nsp14; AltName: Full=Proofreading exoribonuclease nsp14; Short=ExoN;Contains: RecName: Full=Uridylate-specific endoribonuclease nsp15; EC=4.6.1.- ; AltName: Full=NendoU; AltName: Full=Non-structural protein 15; Short=nsp15;Contains: RecName: Full=2'-O-methyltransferase nsp16; EC=2.1.1.57; AltName: Full=Non-structural protein 16; Short=nsp16;

QUERYSEQ

MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELG
TDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRI
RSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNL
LEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAY
ITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTE
VLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEW
SMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAK
KVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVE
QKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCK
SAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEH
FIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSAL
NHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQ
ESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKP
ASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYV
DNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAAL
GVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHV
VDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCE
ESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHIN
AQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKA
CPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVST
SGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICIST
KHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVY
CPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVD
RQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQW
SLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTT
VMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILL
AKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIIN
NARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSD
GTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYV
QIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDG
DMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVD
TDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQ
TVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVA
GVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALL
STDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIER
FVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHK
PPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFV
LTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEI
SMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKIL
GLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFIT
REEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYA
CWHHSIGFDYVYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHMVVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSD
KFTDGVCLFWNCNVDRYPANSIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTR
LQSLENVAFNVVNKGHFDGQQGEVPVSIINNTVYTKVDGVDVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVDIAANTVIWDYKRDAPAHISTIGVCSMTDIAKKPTETICAPLTVFFDGRVDGQVDLFRNARNGVLITEGSV
KGLQPSVGPKQASLNGVTLIGEAVKTQFNYYKKVDGVVQQLPETYFTQSRNLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYGDFSHSQLGGLHLLIGLAKRFKESPFELEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDLL
LDDFVEIIKSQDLSVVSKVVKVTIDYTEISFMLWCKDGHVETFYPKLQSSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLND
FVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQKLALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLSSYSLFDMSKFPL
KLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN

[BLAST file for PDB] (plain) (bar) (multiple alignment) [BLAST for UniProt: (plain) (bar) (multiple alignment) (PSSM file) ]

UniProt Feature Tables [P0DTD1(R1AB_SARS2)]

7096
	region	name	description
	1-7096	CHAIN	/note="Replicase polyprotein 1ab" /id="PRO_0000449618"
	1-180	CHAIN	/note="Host translation inhibitor nsp1" /id="PRO_0000449619"
	181-818	CHAIN	/note="Non-structural protein 2" /id="PRO_0000449620"
	819-2763	CHAIN	/note="Papain-like protease nsp3" /id="PRO_0000449621"
	2764-3263	CHAIN	/note="Non-structural protein 4" /id="PRO_0000449622"
	3264-3569	CHAIN	/note="3C-like proteinase nsp5" /id="PRO_0000449623"
	3570-3859	CHAIN	/note="Non-structural protein 6" /id="PRO_0000449624"
	3860-3942	CHAIN	/note="Non-structural protein 7" /id="PRO_0000449625"
	3943-4140	CHAIN	/note="Non-structural protein 8" /id="PRO_0000449626"
	4141-4253	CHAIN	/note="RNA-capping enzyme subunit nsp9" /id="PRO_0000449627"
	4254-4392	CHAIN	/note="Non-structural protein 10" /id="PRO_0000449628"
	4393-5324	CHAIN	/note="RNA-directed RNA polymerase nsp12" /id="PRO_0000449629"
	5325-5925	CHAIN	/note="Helicase nsp13" /id="PRO_0000449630"
	5926-6452	CHAIN	/note="Guanine-N7 methyltransferase nsp14" /id="PRO_0000449631"
	6453-6798	CHAIN	/note="Uridylate-specific endoribonuclease nsp15" /id="PRO_0000449632"
	6799-7096	CHAIN	/note="2'-O-methyltransferase nsp16" /id="PRO_0000449633"
	1-2225	TOPO_DOM	/note="Cytoplasmic"
	2226-2246	TRANSMEM	/note="Helical"
	2247-2317	TOPO_DOM	/note="Lumenal"
	2318-2338	TRANSMEM	/note="Helical"
	2339-2775	TOPO_DOM	/note="Cytoplasmic"
	2776-2796	TRANSMEM	/note="Helical"
	2797-3044	TOPO_DOM	/note="Lumenal"
	3045-3065	TRANSMEM	/note="Helical"
	3066-3099	TOPO_DOM	/note="Cytoplasmic"
	3100-3120	TRANSMEM	/note="Helical"
	3121-3127	TOPO_DOM	/note="Lumenal"
	3128-3148	TRANSMEM	/note="Helical"
	3149-3586	TOPO_DOM	/note="Cytoplasmic"
	3587-3607	TRANSMEM	/note="Helical"
	3608-3608	TOPO_DOM	/note="Lumenal"
	3609-3629	TRANSMEM	/note="Helical"
	3630-3634	TOPO_DOM	/note="Cytoplasmic"
	3635-3655	TRANSMEM	/note="Helical"
	3656-3673	TOPO_DOM	/note="Lumenal"
	3674-3694	TRANSMEM	/note="Helical"
	3695-3729	TOPO_DOM	/note="Cytoplasmic"
	3730-3750	TRANSMEM	/note="Helical"
	3751-3778	TOPO_DOM	/note="Lumenal"
	3779-3799	TRANSMEM	/note="Helical"
	3800-7096	TOPO_DOM	/note="Cytoplasmic"
	12-127	DOMAIN	/note="CoV Nsp1 globular"
	148-179	DOMAIN	/note="BetaCoV Nsp1 C-terminal"
	183-456	DOMAIN	/note="CoV Nsp2 N-terminal"
	458-688	DOMAIN	/note="CoV Nsp2 middle"
	545-569	REPEAT	/note="LRR 1"
	690-818	DOMAIN	/note="CoV Nsp2 C-terminal"
	697-719	REPEAT	/note="LRR 2"
	821-929	DOMAIN	/note="Ubiquitin-like 1"
	1025-1194	DOMAIN	/note="Macro 1"
	1231-1359	DOMAIN	/note="Macro 2"
	1367-1494	DOMAIN	/note="Macro 3"
	1496-1561	DOMAIN	/note="DPUP"
	1565-1620	DOMAIN	/note="Ubiquitin-like 2"
	1634-1898	DOMAIN	/note="Peptidase C16"
	1680-1702	REPEAT	/note="LRR 3"
	1911-2021	DOMAIN	/note="Nucleic acid-binding"
	2046-2155	DOMAIN	/note="G2M"
	2247-2317	DOMAIN	/note="3Ecto"
	2395-2763	DOMAIN	/note="CoV Nsp3 Y"
	3165-3263	DOMAIN	/note="Nsp4C"
	3185-3206	REPEAT	/note="LRR 4"
	3264-3569	DOMAIN	/note="Peptidase C30"
	3860-3942	DOMAIN	/note="RdRp Nsp7 cofactor"
	3935-3959	REPEAT	/note="LRR 5"
	3943-4140	DOMAIN	/note="RdRp Nsp8 cofactor"
	3977-4004	REPEAT	/note="LRR 6"
	4141-4253	DOMAIN	/note="Nsp9 ssRNA-binding"
	4254-4392	DOMAIN	/note="ExoN/MTase coactivator"
	4399-4653	DOMAIN	/note="NiRAN"
	4591-4616	REPEAT	/note="LRR 7"
	4658-4756	DOMAIN	/note="Nsp12 Interface"
	4757-5324	DOMAIN	/note="Nsp12 RNA-dependent RNA polymerase"
	5004-5166	DOMAIN	/note="RdRp catalytic"
	5325-5408	DOMAIN	/note="CV ZBD"
	5552-5572	REPEAT	/note="LRR 8"
	5581-5762	DOMAIN	/note="(+)RNA virus helicase ATP-binding"
	5763-5932	DOMAIN	/note="(+)RNA virus helicase C-terminal"
	5997-6212	DOMAIN	/note="ExoN"
	6221-6452	DOMAIN	/note="N7-MTase"
	6453-6513	DOMAIN	/note="Nsp15 N-terminal oligomerization"
	6514-6639	DOMAIN	/note="AV-Nsp11N/CoV-Nsp15M"
	6656-6795	DOMAIN	/note="NendoU"
	6800-7094	DOMAIN	/note="Nidovirus-type SAM-dependent 2'-O-MTase"
	6817-6841	REPEAT	/note="LRR 9"
	1752-1789	ZN_FING	/note="C4-type"
	1-147	REGION	/note="Disordered"
	154-180	REGION	/note="Binding to 40s ribosome mRNA entry channel" ECO:0000269\|PubMed:32908316"
	200-236	REGION	/note="C2H2"
	323-344	REGION	/note="C4"
	370-416	REGION	/note="C2HC"
	926-999	REGION	/note="Disordered"
	2395-2485	REGION	/note="Y1"
	2399-2412	REGION	/note="ZF1"
	2445-2455	REGION	/note="ZF2"
	2486-2763	REGION	/note="CoV-Y"
	2486-2580	REGION	/note="Y2"
	2581-2662	REGION	/note="Y3"
	2663-2763	REGION	/note="Y4"
	3931-4020	REGION	/note="Disordered"
	4759-4973	REGION	/note="RdRp Fingers N-ter"
	4937-4947	REGION	/note="Interaction with RMP Remdesivir"
	4974-5012	REGION	/note="RdRp Palm N-ter"
	5013-5071	REGION	/note="RdRp Fingers C-ter"
	5072-5207	REGION	/note="RdRp Palm C-ter"
	5208-5324	REGION	/note="RdRp Thumb"
	6339-6353	REGION	/note="GpppA-binding"
	927-947	COMPBIAS	/note="Acidic residues"
	984-999	COMPBIAS	/note="Polar residues"
	1674-1674	ACT_SITE	/note="For PL-PRO activity" ECO:0000269\|PubMed:32726803"
	1835-1835	ACT_SITE	/note="For PL-PRO activity"
	1849-1849	ACT_SITE	/note="For PL-PRO activity"
	3304-3304	ACT_SITE	/note="For 3CL-PRO activity" ECO:0000305\|PubMed:32198291"
	3408-3408	ACT_SITE	/note="Nucleophile; for 3CL-PRO activity" ECO:0000269\|PubMed:32198291"
	5151-5151	ACT_SITE
	5152-5152	ACT_SITE
	5153-5153	ACT_SITE
	6015-6015	ACT_SITE
	6017-6017	ACT_SITE
	6116-6116	ACT_SITE
	6193-6193	ACT_SITE
	6198-6198	ACT_SITE
	6686-6686	ACT_SITE	/note="Proton donor; for uridylate-specific endoribonuclease nsp15 activity" ECO:0000269\|PubMed:33564093"
	6701-6701	ACT_SITE	/note="Proton acceptor; for uridylate-specific endoribonuclease nsp15 activity" ECO:0000269\|PubMed:33564093"
	6741-6741	ACT_SITE	/note="For uridylate-specific endoribonuclease nsp15 activity"
	6844-6844	ACT_SITE
	6928-6928	ACT_SITE
	6968-6968	ACT_SITE
	7001-7001	ACT_SITE
	200-200	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1"
	231-231	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1"
	234-234	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1"
	236-236	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1"
	323-323	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2"
	326-326	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2"
	341-341	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2"
	344-344	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2"
	370-370	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3"
	373-373	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3"
	382-382	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3"
	416-416	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3"
	1752-1752	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	1755-1755	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	1787-1787	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	1789-1789	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	2399-2399	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	2404-2404	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	2409-2409	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	2412-2412	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	2445-2445	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2448-2448	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2452-2452	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2455-2455	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	4327-4327	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4330-4330	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4336-4336	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4343-4343	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4370-4370	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4373-4373	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4381-4381	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4383-4383	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4601-4601	BINDING	/ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" ECO:0007744\|PDB:7CYQ"
	4610-4610	BINDING	/ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" ECO:0007744\|PDB:7CYQ"
	4687-4687	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="9" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	4693-4693	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="9" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	4698-4698	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="9" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	4702-4702	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="9" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	4879-4879	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="10" /ligand_note="structural" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5034-5034	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="10" /ligand_note="structural" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5037-5037	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="10" /ligand_note="structural" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691"
	5038-5038	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="10" /ligand_note="structural" ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5329-5329	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="11" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5332-5332	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="11" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5340-5340	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="12" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5343-5343	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="11" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5350-5350	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="11" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5353-5353	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="12" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5357-5357	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="12" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5363-5363	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="12" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5374-5374	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="13" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5379-5379	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="13" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5396-5396	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="13" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5399-5399	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="13" ECO:0000269\|PubMed:33232691, ECO:0007744\|PDB:7CYQ"
	5606-5613	BINDING	/ligand="a ribonucleoside 5'-triphosphate" /ligand_id="ChEBI:CHEBI:61557"
	6132-6132	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="14"
	6135-6135	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="14"
	6151-6151	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="14"
	6154-6154	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="14"
	6182-6182	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="15"
	6186-6186	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="15"
	6189-6189	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="15"
	6204-6204	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="15"
	6256-6262	BINDING	/ligand="S-adenosyl-L-methionine" /ligand_id="ChEBI:CHEBI:59789"
	6377-6377	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="16"
	6398-6398	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="16"
	6409-6409	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="16"
	6412-6412	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="16"
	6741-6745	BINDING	/ligand="uracil" /ligand_id="ChEBI:CHEBI:17568" ECO:0000269\|PubMed:33564093"
	6792-6796	BINDING	/ligand="uracil" /ligand_id="ChEBI:CHEBI:17568"
	1-7096	DISORDER	predicted by DISOPRED

MONOMER

7096

pdb_id a¹ identity[%]² description

8gwe A 100.0 R1AB_SARS2 RNA-directed RNA polymerase

7msw A 100.0 R1AB_SARS2 Non-structural protein 2

7egq R 100.0 R1AB_SARS2 Helicase

7egq P 100.0 R1AB_SARS2 Proofreading exoribonuclease

5s72 B 100.0 R1AB_SARS2 Uridylate-specific endoribonuclease

6wuu B 98.8 R1AB_SARS2 Non-structural protein 3

1.a¹:asym_id for the homologue. 2.identity[%]²:sequence identity between the query and the homologue.

HETERO

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

6m71[55] B R1AB_SARS2 Non-structural protein 7[70 aa] A 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

6xez[6] C R1AB_SARS2 Non-structural protein 7[73 aa] E 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

7bw4[1] C R1AB_SARS2 Non-structural protein 7[65 aa] A 100.0
/100.0 10
/10 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] C R1AB_SARS2 Non-structural protein 7[72 aa] A 100.0
/100.0 18
/18 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] C R1AB_SARS2 Non-structural protein 7[72 aa] E 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

6m71[1] C R1AB_SARS2 Non-structural protein 8[43 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

6m71[54] D R1AB_SARS2 Non-structural protein 8[113 aa] A 100.0
/100.0 46
/46 R1AB_SARS2 RNA-directed RNA polymerase

6nur[1] D R1A_CVHSA NSP8[109 aa] A 100.0
/97.0 2
/2 R1AB_CVHSA NSP12

6xez[34] D R1AB_SARS2 Non-structural protein 8[186 aa] A 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

6xez[19] D R1AB_SARS2 Non-structural protein 8[186 aa] E 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

7btf[6] D R1AB_SARS2 Non-structural protein 8[104 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

7bw4[1] B R1AB_SARS2 Non-structural protein 8[115 aa] A 100.0
/100.0 42
/42 R1AB_SARS2 RNA-directed RNA polymerase

7cxm[22] B R1AB_SARS2 Non-structural protein 8[187 aa] H 100.0
/100.0 11
/11 R1AB_SARS2 Helicase

7cxm[3] D R1AB_SARS2 Non-structural protein 8[186 aa] I 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

7cyq[9] B R1AB_SARS2 Non-structural protein 8[187 aa] G 100.0
/100.0 2
/2 R1AB_SARS2 Helicase

7ed5[1] B R1AB_SARS2 Non-structural protein 8[150 aa] A 100.0
/100.0 52
/52 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] D R1AB_SARS2 Non-structural protein 8[154 aa] A 100.0
/100.0 17
/17 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] B R1AB_SARS2 Non-structural protein 8[187 aa] E 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

7egq[1] D R1AB_SARS2 Non-structural protein 8[186 aa] P 100.0
/100.0 1
/1 R1AB_SARS2 Proofreading exoribonuclease

7l1f[1] B R1AB_SARS2 Non-structural protein 8[114 aa] A 100.0
/100.0 40
/40 R1AB_SARS2 RNA-directed RNA polymerase

7rdz[1] D R1AB_SARS2 Non-structural protein 8[185 aa] E 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

7re0[1] B R1AB_SARS2 Non-structural protein 8[186 aa] E 100.0
/100.0 2
/2 R1AB_SARS2 Helicase

7re3[2] G R1AB_SARS2 Non-structural protein 8[186 aa] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

6xa9[2] B ISG15_HUMAN ISG15 CTD-propargylamide[80 aa] A 100.0
/100.0 22
/22 R1AB_SARS2 Non-structural protein 3

6xez[24] E R1AB_SARS2 Helicase[596 aa] A 100.0
/100.0 3
/3 R1AB_SARS2 RNA-directed RNA polymerase

7cxn[1] H R1AB_SARS2 Helicase[596 aa] A 100.0
/99.9 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] M R1AB_SARS2 Helicase[588 aa] H 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease

7re3[2] N R1AB_SARS2 Helicase[590 aa] A 100.0
/100.0 10
/10 R1AB_SARS2 RNA-directed RNA polymerase

6xez[25] A R1AB_SARS2 RNA-directed RNA polymerase[926 aa] E 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

7cxn[1] A R1AB_SARS2 RNA-directed RNA polymerase[926 aa] H 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

7egq[2] A R1AB_SARS2 RNA-directed RNA polymerase[926 aa] E 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

7egq[2] I R1AB_SARS2 RNA-directed RNA polymerase[926 aa] H 100.0
/100.0 17
/17 R1AB_SARS2 Proofreading exoribonuclease

7re3[2] J R1AB_SARS2 RNA-directed RNA polymerase[927 aa] F 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

6xqb[1] D R1AB_SARS2 Non-structural protein 8[31 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

7aap[2] D R1AB_SARS2 Non-structural protein 8[28 aa] A 100.0
/100.0 2
/2 R1AB_SARS2 Non-structural protein 12

7bv1[1] D R1AB_SARS2 Non-structural protein 8[99 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

7cyq[11] I R1AB_SARS2 Non-structural protein 9[113 aa] A 100.0
/100.0 19
/19 R1AB_SARS2 RNA-directed RNA polymerase

7egq[3] F R1AB_SARS2 Non-structural protein 9[113 aa] H 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease

7egq[3] H R1AB_SARS2 Proofreading exoribonuclease[523 aa] A 100.0
/100.0 2
/2 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] P R1AB_SARS2 Proofreading exoribonuclease[524 aa] A 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] P R1AB_SARS2 Proofreading exoribonuclease[524 aa] E 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

7oyg[2] B R1AB_SARS2 SARS-CoV-2 nsp8[81 aa] A 100.0
/100.0 28
/28 R1AB_SARS2 SARS-CoV-2 RNA-dependent RNA polymerase (nsp12)

7thm[1] C R1AB_SARS2 Non-structural protein 7[37 aa] A 100.0
/100.0 7
/7 R1AB_SARS2 RNA-directed RNA polymerase

7thm[1] E R1AB_SARS2 Non-structural protein 9[74 aa] A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

8cx9[6] G RL40_HUMAN Ubiquitin variant UbV.CV2.1[75 aa] A 100.0
/100.0 12
/12 R1A_SARS2 Papain-like protease nsp3

5c8s[15] A R1AB_CVHSA Non-structural protein 10[133 aa] B 98.0
/94.9 49
/49 R1AB_CVHSA Guanine-N7 methyltransferase

5nfy[4] E Q1T6X8_CVHSA Polyprotein 1ab[132 aa] A 98.0
/94.7 50
/50 Q1T6X8_CVHSA Polyprotein 1ab

7n0d[2] C R1AB_SARS2 Non-structural protein 10[131 aa] B 100.0
/99.8 4
/4 R1AB_SARS2 Proofreading exoribonuclease

7rbs[2] H ISG15_HUMAN Ubiquitin-like protein ISG15[157 aa] G 96.4
/99.7 28
/28 R1A_SARS2 Papain-like protease

6wuu[5] E VIR250[5 aa] A 100.0
/99.7 18
/18 R1AB_SARS2 Non-structural protein 3

8g6r[1] B A0A1Z2R8Q6_9ALPC nsp8[114 aa] A 53.5
/60.9 43
/44 A0A0U2C263_9ALPC nsp12

8g6r[1] C A0A0M4AW09_9ALPC nsp7[62 aa] A 81.2
/60.9 16
/16 A0A0U2C263_9ALPC nsp12

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

NUCLEOTIDE

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

6x1b[6] C DNA (5'-R(*GP*U)-3') A 100.0
/100.0 11
/11 R1AB_SARS2 Uridylate-specific endoribonuclease

6xez[9] G Product RNA A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

6xez[1] H Template RNA A 100.0
/100.0 21
/21 R1AB_SARS2 RNA-directed RNA polymerase

6xqb[1] E RNA (5'-R(*GP*UP*GP*GP*GP*CP*CP*CP*A)-3') A 100.0
/100.0 15
/15 R1AB_SARS2 RNA-directed RNA polymerase

6xqb[1] F RNA (5'-R(*GP*UP*GP*GP*GP*CP*CP*CP*A)-3') A 100.0
/100.0 19
/19 R1AB_SARS2 RNA-directed RNA polymerase

6yyt[1] E RNA product A 100.0
/100.0 14
/14 R1AB_SARS2 nsp12

6yyt[1] G RNA product A 100.0
/100.0 26
/26 R1AB_SARS2 nsp12

7aap[1] E RNA (5'-R(P*UP*UP*AP*AP*GP*UP*UP*AP*U)-3') A 100.0
/100.0 16
/16 R1AB_SARS2 Non-structural protein 12

7aap[1] F RNA (5'-R(P*UP*UP*CP*AP*UP*AP*AP*CP*UP*UP*AP*A)-3'.. A 100.0
/100.0 23
/23 R1AB_SARS2 Non-structural protein 12

7b3b[1] D DNA/RNA (5'-R(P*CP*UP*AP*CP*GP*CP*G)-D(P*(RMP))-R(.. A 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase nsp12

7b3b[1] E RNA (5'-R(P*UP*GP*CP*AP*UP*CP*GP*CP*GP*UP*AP*G)-3'.. A 100.0
/100.0 28
/28 R1AB_SARS2 RNA-directed RNA polymerase nsp12

7b3c[1] D DNA/RNA (5'-R(P*CP*UP*AP*CP*GP*CP*A)-D(P*(RMP))-R(.. A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase nsp12

7b3c[1] E RNA (5'-R(P*UP*CP*AP*CP*UP*UP*GP*CP*GP*UP*AP*G)-3'.. A 100.0
/100.0 26
/26 R1AB_SARS2 RNA-directed RNA polymerase nsp12

7b3d[3] D RNA (5'-R(P*CP*UP*AP*CP*GP*CP*AP*GP*UP*G)-3') A 100.0
/100.0 14
/14 R1AB_SARS2 SARS-CoV-2 RNA-dependent RNA polymerase nsp12

7b3d[3] E RNA (5'-R(P*UP*GP*CP*AP*CP*UP*GP*CP*GP*UP*AP*G)-3'.. A 100.0
/100.0 29
/29 R1AB_SARS2 SARS-CoV-2 RNA-dependent RNA polymerase nsp12

7bv2[1] D Primer A 100.0
/100.0 15
/15 R1AB_SARS2 RNA-directed RNA polymerase

7bv2[1] E Templete A 100.0
/100.0 26
/26 R1AB_SARS2 RNA-directed RNA polymerase

7bzf[1] E RNA (31-MER) A 100.0
/100.0 25
/25 R1AB_SARS2 RNA-directed RNA polymerase

7bzf[1] F RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*CP*AP*CP*.. A 100.0
/100.0 13
/13 R1AB_SARS2 RNA-directed RNA polymerase

7c2k[1] E RNA (29-MER) A 100.0
/100.0 24
/24 R1AB_SARS2 RNA-directed RNA polymerase

7c2k[1] F RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*CP*AP*CP*.. A 100.0
/100.0 17
/17 R1AB_SARS2 RNA-directed RNA polymerase

7ctt[1] E Primer-RNA (5'-R(P*UP*UP*CP*UP*CP*CP*UP*AP*AP*GP*A.. A 100.0
/100.0 18
/18 R1AB_SARS2 RNA-directed RNA polymerase

7ctt[1] F Template-RNA (5'-R(P*AP*CP*UP*AP*GP*CP*UP*UP*CP*UP.. A 100.0
/100.0 25
/25 R1AB_SARS2 RNA-directed RNA polymerase

7cxm[12] E RNA (25-MER) A 100.0
/99.9 10
/10 R1AB_SARS2 RNA-directed RNA polymerase

7cxm[2] G RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') I 100.0
/100.0 20
/20 R1AB_SARS2 Helicase

7cyq[1] E Primer A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

7cyq[1] F Template A 100.0
/100.0 30
/30 R1AB_SARS2 RNA-directed RNA polymerase

7dfg[2] A RNA (5'-R(P*AP*GP*AP*UP*UP*AP*AP*GP*UP*UP*AP*U)-3'.. C 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase

7dfg[1] B RNA (5'-R(P*CP*CP*CP*UP*AP*UP*AP*AP*CP*UP*UP*AP*AP.. C 100.0
/100.0 30
/30 R1AB_SARS2 RNA-directed RNA polymerase

7dfh[1] E RNA (5'-R(P*GP*CP*UP*AP*UP*GP*UP*G*(LIG))-3') A 100.0
/100.0 13
/13 R1AB_SARS2 RNA-directed RNA polymeras

7dfh[1] F RNA (5'-R(P*CP*CP*CP*CP*CP*AP*CP*AP*UP*AP*GP*C)-3'.. A 100.0
/100.0 24
/24 R1AB_SARS2 RNA-directed RNA polymeras

7doi[1] E RNA (5'-R(P*CP*CP*UP*AP*UP*AP*AP*CP*UP*UP*AP*AP*UP.. A 100.0
/100.0 28
/28 R1AB_SARS2 RNA-directed RNA polymerase

7dok[1] A RNA (5'-R(P*GP*CP*UP*AP*UP*GP*UP*GP*AP*GP*AP*UP*UP.. C 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] E RNA (5'-R(P*GP*CP*UP*AP*UP*GP*UP*GP*AP*GP*AP*UP*UP.. A 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

7dok[1] B RNA (5'-R(P*CP*CP*CP*UP*AP*UP*AP*AP*CP*UP*UP*AP*AP.. C 100.0
/100.0 26
/26 R1AB_SARS2 RNA-directed RNA polymerase

7dte[1] E RNA (57-MER) A 100.0
/100.0 27
/27 R1AB_SARS2 RNA-directed RNA polymerase

7dte[1] F RNA (33-MER) A 100.0
/100.0 15
/15 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] F RNA (5'-R(P*CP*CP*CP*CP*AP*UP*AP*AP*CP*UP*UP*AP*AP.. A 100.0
/100.0 28
/28 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] T Template RNA A 100.0
/100.0 27
/27 R1AB_SARS2 RNA-directed RNA polymerase

7egq[1] T Template RNA E 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

7eiz[1] H template A 100.0
/100.0 21
/21 R1AB_SARS2 RNA-directed RNA polymerase

7krn[3] F RNA (37-MER) A 100.0
/100.0 20
/20 R1AB_SARS2 RNA-directed RNA polymerase

7krn[2] G RNA (43-MER) A 100.0
/100.0 27
/27 R1AB_SARS2 RNA-directed RNA polymerase

7krn[2] G RNA (43-MER) E 100.0
/100.0 32
/32 R1AB_SARS2 Helicase

7krp[1] F RNA (36-MER) A 100.0
/100.0 28
/28 R1AB_SARS2 RNA-directed RNA polymerase

7l1f[1] D RNA (5'-R(P*CP*UP*AP*AP*GP*AP*AP*GP*CP*UP*AP*UP*U*.. A 100.0
/100.0 17
/17 R1AB_SARS2 RNA-directed RNA polymerase

7l1f[1] E RNA (5'-R(P*AP*UP*UP*UP*UP*AP*AP*UP*AP*GP*CP*UP*UP.. A 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase

7n06[6] G RNA (5'-R(*AP*UP*A)-3') A 100.0
/100.0 10
/10 R1AB_SARS2 Uridylate-specific endoribonuclease

7n06[3] H RNA (5'-R(*AP*UP*A)-3') A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7n0b[1] C RNA (5'-R(*AP*UP*GP*UP*GP*AP*UP*UP*UP*UP*AP*AP*UP*.. B 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease

7n0b[1] D RNA (5'-R(*AP*GP*AP*AP*GP*CP*UP*AP*UP*UP*AP*AP*AP*.. B 100.0
/100.0 15
/15 R1AB_SARS2 Proofreading exoribonuclease

7n33[6] G RNA (5'-R(*A)-D(*(UFT))-R(P*A)-3') A 100.0
/100.0 11
/11 R1AB_SARS2 Uridylate-specific endoribonuclease

7ozu[1] D Product RNA A 100.0
/100.0 14
/14 R1AB_SARS2 Replicase polyprotein 1ab

7ozu[2] E Template RNA A 100.0
/100.0 30
/30 R1AB_SARS2 Replicase polyprotein 1ab

7ozv[1] D Product RNA A 100.0
/100.0 12
/12 R1AB_SARS2 Replicase polyprotein 1ab

7rdx[1] H Template RNA A 100.0
/100.0 34
/34 R1AB_SARS2 RNA-directed RNA polymerase

7rdx[1] H Template RNA E 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

7rdy[1] H Template RNA A 100.0
/100.0 32
/32 R1AB_SARS2 RNA-directed RNA polymerase

7rdy[1] H Template RNA E 100.0
/100.0 30
/30 R1AB_SARS2 Helicase

7rdz[6] H Template RNA A 100.0
/100.0 31
/31 R1AB_SARS2 RNA-directed RNA polymerase

7uo4[1] E Product RNA (35-MER) A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

7uo4[1] F Template RNA (55-MER) A 100.0
/100.0 28
/28 R1AB_SARS2 RNA-directed RNA polymerase

7uo7[1] D Product RNA (35-MER) A 100.0
/100.0 17
/17 R1AB_SARS2 RNA-directed RNA polymerase

7uo7[1] E Template RNA (55-MER) A 100.0
/100.0 27
/27 R1AB_SARS2 RNA-directed RNA polymerase

7uo9[1] D Product RNA (35-MER) A 100.0
/100.0 13
/13 R1AB_SARS2 RNA-directed RNA polymerase

7uo9[1] E Template RNA (55-MER) A 100.0
/100.0 34
/34 R1AB_SARS2 RNA-directed RNA polymerase

7uob[2] E Product RNA (35-MER) A 100.0
/100.0 10
/10 R1AB_SARS2 RNA-directed RNA polymerase

7uob[1] F Template RNA (55-MER) A 100.0
/100.0 24
/24 R1AB_SARS2 RNA-directed RNA polymerase

7uoe[1] F Template RNA (55-MER) A 100.0
/100.0 30
/30 R1AB_SARS2 RNA-directed RNA polymerase

8gwb[7] F template A 100.0
/100.0 26
/26 R1AB_SARS2 RNA-directed RNA polymerase

8gwb[5] F template G 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

8gwb[1] J RNA (5'-R(P*AP*U)-3') A 100.0
/100.0 10
/10 R1AB_SARS2 RNA-directed RNA polymerase

8gwe[1] J RNA (5'-R(P*AP*UP*UP*A)-3') A 100.0
/100.0 15
/15 R1AB_SARS2 RNA-directed RNA polymerase

7cxm[2] F RNA (26-MER) A 100.0
/99.9 23
/23 R1AB_SARS2 RNA-directed RNA polymerase

7n0c[1] C RNA (25-MER) B 100.0
/99.8 10
/10 R1AB_SARS2 Proofreading exoribonuclease

7n0c[1] D RNA (24-MER) B 100.0
/99.8 18
/18 R1AB_SARS2 Proofreading exoribonuclease

7n0d[4] E RNA (5'-R(*GP*GP*GP*GP*AP*UP*GP*UP*GP*AP*UP*UP*UP*.. B 100.0
/99.8 9
/9 R1AB_SARS2 Proofreading exoribonuclease

7n0d[2] F RNA (5'-R(*CP*UP*AP*UP*UP*AP*AP*AP*AP*UP*CP*AP*CP*.. B 100.0
/99.8 16
/16 R1AB_SARS2 Proofreading exoribonuclease

7n0d[2] G RNA (5'-R(*CP*CP*CP*CP*C)-3') B 100.0
/99.8 1
/1 R1AB_SARS2 Proofreading exoribonuclease

7n0d[2] G RNA (5'-R(*CP*CP*CP*CP*C)-3') D 100.0
/99.8 15
/15 R1AB_SARS2 Proofreading exoribonuclease

7tj2[1] G RNA (31-MER) A 100.0
/99.7 11
/11 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] G RNA (31-MER) C 100.0
/99.7 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] G RNA (31-MER) E 100.0
/99.7 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] H RNA (31-MER) A 100.0
/99.7 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] H RNA (31-MER) C 100.0
/99.7 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] H RNA (31-MER) E 100.0
/99.7 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tqv[1] G RNA (33-MER) A 100.0
/99.7 11
/11 R1AB_SARS2 Uridylate-specific endoribonuclease

7tqv[1] G RNA (33-MER) C 100.0
/99.7 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7tqv[1] G RNA (33-MER) E 100.0
/99.7 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7tqv[1] H RNA (33-MER) A 100.0
/99.7 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

7tqv[1] H RNA (33-MER) C 100.0
/99.7 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7tqv[1] H RNA (33-MER) E 100.0
/99.7 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

8g6r[1] D RNA (5'-R(P*AP*AP*GP*AP*AP*GP*CP*UP*AP*UP*UP*AP*AP.. A 93.8
/60.9 16
/16 A0A0U2C263_9ALPC nsp12

8g6r[1] E RNA (5'-R(P*GP*GP*UP*UP*GP*UP*GP*AP*UP*UP*UP*UP*AP.. A 77.8
/60.9 27
/27 A0A0U2C263_9ALPC nsp12

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

COMPOUND

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

5rl6[1] H LJA
N-[3-(carbamoylamino)phenyl]acetamide[14 atoms] B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5slf[1] G LJA
N-[3-(carbamoylamino)phenyl]acetamide[14 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slf[1] H LJA
N-[3-(carbamoylamino)phenyl]acetamide[14 atoms] A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5rl7[1] C VVD
5-(acetylamino)-2-fluorobenzoic acid[14 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rl7[1] I VVD
5-(acetylamino)-2-fluorobenzoic acid[14 atoms] B 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rl8[1] C VVG
N-(2-fluorophenyl)ethanesulfonamide[13 atoms] A 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

5rl8[1] D VVG
N-(2-fluorophenyl)ethanesulfonamide[13 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rl9[1] H UR7
1-(3-fluoro-4-methylphenyl)methanesulfonamide[13 a.. B 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rlb[1] C VVJ
N-cycloheptyl-N-methylmethanesulfonamide[13 atoms].. A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rlc[1] H VVM
4-amino-N-phenylbenzene-1-sulfonamide[17 atoms] B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rld[1] H VVY
2-phenoxy-1-(pyrrolidin-1-yl)ethan-1-one[15 atoms].. B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rle[1] H VVP
4-methoxy-1H-indole[11 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rlf[1] C NY7
N-(2-methoxy-5-methylphenyl)glycinamide[14 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rlg[1] C VW1
(2S)-2-(4-cyanophenoxy)propanamide[14 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rlh[1] H K2P
2-(trifluoromethoxy)benzoic acid[14 atoms] B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rli[2] C JFM
N-(2-phenylethyl)methanesulfonamide[13 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rli[1] I JFM
N-(2-phenylethyl)methanesulfonamide[13 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rlj[1] H VW4
(2S)-2-phenylpropane-1-sulfonamide[13 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rlk[1] H NYV
1-(propan-2-yl)-1H-imidazole-4-sulfonamide[12 atom.. B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rll[1] H H04
1-(2-ethoxyphenyl)piperazine[15 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rlm[1] H VW7
N-(8-methyl-1,2,3,4-tetrahydroquinolin-5-yl)acetam.. B 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

5rln[1] C NZG
3-(acetylamino)-4-fluorobenzoic acid[14 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rlo[1] H UQS
N-[(2-fluorophenyl)methyl]-1H-pyrazol-4-amine[14 a.. B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rlp[1] H VWA
(1S)-1-(4-fluorophenyl)-N-methylethan-1-amine[11 a.. B 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rlq[1] C UVA
N-methyl-2-(methylsulfonyl)aniline[12 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rlr[1] H VWD
(1R)-2-(methylsulfonyl)-1-phenylethan-1-ol[13 atom.. B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rls[1] C VWG
N-hydroxyquinoline-2-carboxamide[14 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5sac[3] E VWG
N-hydroxyquinoline-2-carboxamide[14 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5rlt[1] H UVJ
3-(2-methyl-1H-benzimidazol-1-yl)propanamide[15 at.. B 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rlu[1] C JG4
2-(thiophen-2-yl)-1H-imidazole[10 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

5rlu[1] I JG4
2-(thiophen-2-yl)-1H-imidazole[10 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rlv[1] C VWJ
N-(propan-2-yl)-1H-benzimidazol-2-amine[13 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rlv[1] D VWJ
N-(propan-2-yl)-1H-benzimidazol-2-amine[13 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rlv[1] J VWJ
N-(propan-2-yl)-1H-benzimidazol-2-amine[13 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rlw[1] C S9S
~{N}-[2-(4-fluorophenyl)ethyl]methanesulfonamide[1.. A 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rlw[1] I S9S
~{N}-[2-(4-fluorophenyl)ethyl]methanesulfonamide[1.. B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rly[1] C K34
5-(1,3-thiazol-2-yl)-1H-1,2,4-triazole[10 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rly[1] I K34
5-(1,3-thiazol-2-yl)-1H-1,2,4-triazole[10 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rly[1] J K34
5-(1,3-thiazol-2-yl)-1H-1,2,4-triazole[10 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rlz[1] C VWM
(3R)-1-acetyl-3-hydroxypiperidine-3-carboxylic aci.. A 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rm0[1] H S7G
~{N}-[(3~{R})-1,2,3,4-tetrahydroquinolin-3-yl]etha.. B 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rm1[1] H RY4
N-[4-(aminomethyl)phenyl]methanesulfonamide[13 ato.. B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rm2[1] H UXG
1-(diphenylmethyl)azetidin-3-ol[18 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rm2[1] I UXG
1-(diphenylmethyl)azetidin-3-ol[18 atoms] B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rm3[1] C S7J
2-(trifluoromethyl)pyrimidine-5-carboxamide[13 ato.. A 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rm4[1] H PK4
2-fluoro-N,3-dimethylbenzene-1-sulfonamide[13 atom.. B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rm5[1] H NUA
N-(1-ethyl-1H-pyrazol-4-yl)cyclobutanecarboxamide[.. B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rm6[1] H HR5
~{N}-(cyclobutylmethyl)-1,5-dimethyl-pyrazole-4-ca.. B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rm7[1] H N0E
~{N}-(4-hydroxyphenyl)-3-phenyl-propanamide[18 ato.. B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rm8[1] C GQJ
methyl (2~{S},4~{R})-1-(furan-2-ylcarbonyl)-4-oxid.. A 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rm9[1] H EJQ
~{N}-(4-fluorophenyl)-2-pyrrolidin-1-yl-ethanamide.. B 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

5slv[1] G EJQ
~{N}-(4-fluorophenyl)-2-pyrrolidin-1-yl-ethanamide.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5rma[1] H JHJ
N-(4-methoxyphenyl)-N'-pyridin-4-ylurea[18 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rmb[1] C VWV
ethyl (1,1-dioxo-1lambda~6~,4-thiazinan-4-yl)aceta.. A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5rmc[1] H 6SU
methyl 3-(methylsulfonylamino)benzoate[15 atoms] B 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rmd[2] C VWY
N-ethyl-4-[(methylsulfonyl)amino]benzamide[16 atom.. A 100.0
/100.0 9
/9 R1AB_SARS2 Helicase

5rme[1] C RYM
4-(benzimidazol-1-ylmethyl)benzenecarbonitrile[18 .. A 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rmf[1] C NX7
(2,6-difluorophenyl)(pyrrolidin-1-yl)methanone[15 .. A 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rmg[1] H MUK
4,6-dimethyl-~{N}-phenyl-pyrimidin-2-amine[15 atom.. B 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rmh[1] C VX4
[(4S)-4-methylazepan-1-yl](1,3-thiazol-4-yl)methan.. A 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

5rmi[1] C STV
~{N}-(1,3-benzodioxol-5-ylmethyl)ethanesulfonamide.. A 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

5rmj[1] C JOV
3-chloro-N-(1-hydroxy-2-methylpropan-2-yl)benzamid.. A 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

5sa8[6] C JOV
3-chloro-N-(1-hydroxy-2-methylpropan-2-yl)benzamid.. A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa8[3] C JOV
3-chloro-N-(1-hydroxy-2-methylpropan-2-yl)benzamid.. A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa8[3] D JOV
3-chloro-N-(1-hydroxy-2-methylpropan-2-yl)benzamid.. B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

5rmk[1] H O2A
N-methyl-1H-indole-7-carboxamide[13 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

5sl1[1] G O2A
N-methyl-1H-indole-7-carboxamide[13 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5rml[1] H VXD
N-(3-chloro-2-methylphenyl)glycinamide[13 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Helicase

5rmm[1] H VXG
(3S,4R)-1-acetyl-4-phenylpyrrolidine-3-carboxylic .. B 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

5s6x[6] D WUG
1-(2,4-dimethyl-1H-imidazol-5-yl)methanamine[9 ato.. A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6y[3] D WUJ
N-[(furan-2-yl)methyl]urea[10 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6y[3] F WUJ
N-[(furan-2-yl)methyl]urea[10 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6z[6] D WUM
4-[(dimethylamino)methyl]-1,3-thiazol-2-amine[10 a.. A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

5s70[3] E WUS
(5R)-2-methyl-4,5,6,7-tetrahydro-1H-benzimidazol-5.. B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

5s71[6] D WUV
5'-thiothymidine[17 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

5s71[6] D WUV
5'-thiothymidine[17 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5s72[3] D WUY
N-(2-aminoethyl)-N'-phenylurea[13 atoms] A 100.0
/100.0 10
/10 R1AB_SARS2 Uridylate-specific endoribonuclease

5s72[3] D WUY
N-(2-aminoethyl)-N'-phenylurea[13 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa4[3] C K3A
N-(5-methyl-1H-pyrazol-3-yl)acetamide[10 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa5[3] E ZQA
4-ethyl-2-(1H-imidazol-5-yl)-1,3-thiazole[12 atoms.. B 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa6[6] C O3G
N-benzyl-1-(4-fluorophenyl)methanamine[16 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa6[6] C O3G
N-benzyl-1-(4-fluorophenyl)methanamine[16 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa7[6] C WL7
4-amino-N-(2-hydroxyethyl)-N-methylbenzene-1-sulfo.. A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

5sa9[3] C GWG
1-methylindazole-3-carboxamide[13 atoms] B 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

5saa[6] D ZQD
3-[(2S)-1-(methanesulfonyl)pyrrolidin-2-yl]-5-meth.. A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

5sab[3] E WJD
2-methoxy-N-phenylacetamide[12 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5sad[3] C EJW
(3-phenyl-1,2-oxazol-5-yl)methylazanium[13 atoms] B 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

5sae[6] D W3G
pyridazin-3(2H)-one[7 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

5saf[6] D WOY
6,7-dihydro-5H-pyrrolo[2,3-d]pyrimidine[9 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

5sag[3] C ZQG
3-(1H-imidazol-2-yl)propan-1-amine[9 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

5sag[3] C ZQG
3-(1H-imidazol-2-yl)propan-1-amine[9 atoms] B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

5sah[3] C ZQJ
2-methyl-5,6,7,8-tetrahydropyrido[4,3-c]pyridazin-.. A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

5sah[3] D ZQJ
2-methyl-5,6,7,8-tetrahydropyrido[4,3-c]pyridazin-.. B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

5sai[3] C ZQM
N-{2-[(propan-2-yl)sulfanyl]phenyl}urea[14 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

5skw[1] B LF6
{(1R,2R)-2-[(Z)-(3-methyl-1,2,4-thiadiazol-5(2H)-y.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5skx[1] B T6J
2-[(methylsulfonyl)methyl]-1H-benzimidazole[14 ato.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sky[1] G O2M
N-[(4-methyl-1,3-thiazol-2-yl)methyl]-1H-pyrazole-.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5skz[1] G NVD
N-{[4-(dimethylamino)phenyl]methyl}-4H-1,2,4-triaz.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl0[1] G B0V
2-methoxy-~{N}-(2,4,6-trimethylphenyl)ethanamide[1.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl0[1] H B0V
2-methoxy-~{N}-(2,4,6-trimethylphenyl)ethanamide[1.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl2[1] G LFO
N,1-dimethyl-1H-indole-3-carboxamide[14 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl3[1] G LGR
2-[acetyl(methyl)amino]benzoic acid[14 atoms] A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl4[1] G LHR
N-(1H-indazol-6-yl)acetamide[13 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl4[1] H LHR
N-(1H-indazol-6-yl)acetamide[13 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl5[1] G WNV
N,N,2,3-tetramethylbenzamide[13 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl6[1] G 60P
3-methylthiophene-2-carboxylic acid[9 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl6[1] H 60P
3-methylthiophene-2-carboxylic acid[9 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl7[1] G W0G
(3R)-1-(2-fluorophenyl)-3-(methylamino)pyrrolidin-.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl8[1] G JGD
N,N-dimethylpyridin-4-amine[9 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sl9[1] G O0S
N-{4-[(pyrimidin-2-yl)oxy]phenyl}acetamide[17 atom.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sla[1] G LJR
1-cyclohexyl-N-methylmethanesulfonamide[12 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sla[1] H LJR
1-cyclohexyl-N-methylmethanesulfonamide[12 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slb[1] G LJK
3-methyl-N-(2-methylbutan-2-yl)-1H-pyrazole-5-carb.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slc[1] G U1V
1-(4-fluoro-2-methylphenyl)methanesulfonamide[13 a.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sld[1] G LJ6
(2R)-3-(3,5-dimethyl-1,2-oxazol-4-yl)-N,N,2-trimet.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sle[1] G JGA
N-ethyl-N'-(5-methyl-1,2-oxazol-3-yl)urea[12 atoms.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sle[1] H JGA
N-ethyl-N'-(5-methyl-1,2-oxazol-3-yl)urea[12 atoms.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slg[1] G NZJ
1-(3-methylbenzene-1-carbonyl)piperidine-4-carboxa.. A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slh[1] G LLU
(2S)-2-(2-fluorophenoxy)propanoic acid[13 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sli[1] G LL0
2-(difluoromethoxy)benzene-1-sulfonamide[14 atoms].. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sli[1] H LL0
2-(difluoromethoxy)benzene-1-sulfonamide[14 atoms].. A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sli[1] I LL0
2-(difluoromethoxy)benzene-1-sulfonamide[14 atoms].. A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slj[1] G LKU
3-fluoro-N-(3-hydroxy-4-methylphenyl)benzamide[18 .. A 100.0
/100.0 12
/12 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slk[1] G LKL
2-[(5-chloro-3-fluoropyridin-2-yl)(methyl)amino]et.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sll[1] G LK6
N-[(3R)-3-methyl-1,1-dioxo-1lambda~6~-thiolan-3-yl.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slm[1] G WN1
N-(2-fluorophenyl)-3-methoxybenzamide[18 atoms] A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sln[1] G LUY
~{N}-(2-phenylethyl)-1~{H}-benzimidazol-2-amine[18.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slo[1] G JJM
1-methyl-N-(3-methylphenyl)-1H-pyrazolo[3,4-d]pyri.. A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slp[1] G UWY
N-(1-ethyl-1H-pyrazol-4-yl)cyclopentanecarboxamide.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slq[1] G ELQ
[3,4-bis(fluoranyl)phenyl]-(4-methylpiperazin-1-yl.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slr[1] G LO6
2-(difluoromethoxy)-1-[(2R,6S)-2,6-dimethylmorphol.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sls[1] G SZE
4-(3-fluoranylpyridin-2-yl)-1-methyl-piperazin-2-o.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slt[1] G LNS
6-(methylcarbamoyl)pyridine-2-carboxylic acid[13 a.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slu[1] G UX1
1-[(2-fluorophenyl)methyl]-N-methylcyclopropane-1-.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slu[1] H UX1
1-[(2-fluorophenyl)methyl]-N-methylcyclopropane-1-.. A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slw[1] G U0V
2-fluoro-N-[2-(pyridin-4-yl)ethyl]benzamide[18 ato.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slw[1] H U0V
2-fluoro-N-[2-(pyridin-4-yl)ethyl]benzamide[18 ato.. A 100.0
/100.0 12
/12 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slx[1] G LMW
2-[(4-aminophenyl)(ethyl)amino]ethan-1-ol[13 atoms.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slx[1] H LMW
2-[(4-aminophenyl)(ethyl)amino]ethan-1-ol[13 atoms.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sly[1] G LM6
1-(1-ethyl-1H-pyrazol-5-yl)-N-methylmethanamine[10.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5slz[1] G LQP
2-(difluoromethoxy)-1-[(3aR,6aS)-hexahydrocyclopen.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm0[1] G LQI
(1-benzofuran-2-yl)(4-methylpiperidin-1-yl)methano.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm1[1] G WH1
N-methyl-N-[2-(pyridin-2-yl)ethyl]benzamide[18 ato.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm2[1] G LQ3
(5S)-5-(difluoromethoxy)pyridin-2(5H)-one[11 atoms.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm2[1] H LQ3
(5S)-5-(difluoromethoxy)pyridin-2(5H)-one[11 atoms.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm3[1] G GT4
~{N}-(4-hydroxyphenyl)-2-methoxy-ethanamide[13 ato.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm4[1] G AWD
~{N}-(4-fluorophenyl)-4-methyl-piperazine-1-carbox.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm5[1] G S5J
2-[4-(2-methoxyphenyl)piperazin-1-yl]ethanenitrile.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm6[1] G K1A
3-[(3,5-dimethyl-1,2-oxazol-4-yl)methyl]-5-methyl-.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm7[1] G LPU
1-(methanesulfonyl)piperidin-4-ol[11 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm8[1] G WKA
N-(2,1,3-benzoxadiazol-4-yl)acetamide[13 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sm9[1] G VZS
N-(2-methoxy-5-methylphenyl)-N'-4H-1,2,4-triazol-4.. A 100.0
/100.0 12
/12 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sma[1] G NZD
4-methyl-N-phenylpiperazine-1-carboxamide[16 atoms.. A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smb[1] G LRR
1-(morpholin-4-yl)-4-phenylbutan-1-one[17 atoms] A 100.0
/100.0 10
/10 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smc[1] G LRF
N~2~-(4-cyano-3-methyl-1,2-thiazol-5-yl)-N~2~-meth.. A 100.0
/100.0 11
/11 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smc[1] H LRF
N~2~-(4-cyano-3-methyl-1,2-thiazol-5-yl)-N~2~-meth.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smd[1] G WKS
2,4-dimethyl-6-(piperazin-1-yl)pyrimidine[14 atoms.. A 100.0
/100.0 6
/6 R1AB_SARS2 Proofreading exoribonuclease nsp14

5sme[1] G I8D
(4-chlorophenyl)(thiomorpholin-4-yl)methanone[15 a.. A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smf[1] G K1S
N,N-diethyl-5-methyl[1,2,4]triazolo[1,5-a]pyrimidi.. A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smf[1] H K1S
N,N-diethyl-5-methyl[1,2,4]triazolo[1,5-a]pyrimidi.. A 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smg[1] G LR9
3-amino-N-ethyl-N-methylbenzamide[13 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smh[1] G 7ZC
1-(5-methoxy-1H-indol-3-yl)-N,N-dimethyl-methanami.. A 100.0
/100.0 7
/7 R1AB_SARS2 Proofreading exoribonuclease nsp14

5smi[1] G LQV
(2S)-N-(5-methylpyridin-2-yl)oxolane-2-carboxamide.. A 100.0
/100.0 8
/8 R1AB_SARS2 Proofreading exoribonuclease nsp14

6wlc[6] C U5P
URIDINE-5'-MONOPHOSPHATE[21 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

7k0r[6] G U5P
URIDINE-5'-MONOPHOSPHATE[21 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[6] C CMU
5-CHLORO-6-(1-(2-IMINOPYRROLIDINYL) METHYL) URACIL.. A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[6] C U3P
3'-URIDINEMONOPHOSPHATE[21 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

6xez[12] L ADP
ADENOSINE-5'-DIPHOSPHATE[27 atoms] A 100.0
/100.0 11
/11 R1AB_SARS2 RNA-directed RNA polymerase

6xez[18] R ADP
ADENOSINE-5'-DIPHOSPHATE[27 atoms] E 100.0
/100.0 10
/10 R1AB_SARS2 Helicase

6xez[8] M 1N7
CHAPSO[35 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 RNA-directed RNA polymerase

6xez[8] N 1N7
CHAPSO[26 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

6xez[10] U 1N7
CHAPSO[36 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 RNA-directed RNA polymerase

6xez[9] U 1N7
CHAPSO[36 atoms] E 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

7n0d[4] LA 1N7
CHAPSO[25 atoms] B 100.0
/99.8 5
/5 R1AB_SARS2 Proofreading exoribonuclease

7aap[2] M GE6
[[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonyl-5-f.. A 100.0
/100.0 7
/7 R1AB_SARS2 Non-structural protein 12

7bv2[1] K F86
[(2~{R},3~{S},4~{R},5~{R})-5-(4-azanylpyrrolo[2,1-.. A 100.0
/100.0 7
/7 R1AB_SARS2 RNA-directed RNA polymerase

7cjm[3] B TTT
5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]be.. A 100.0
/99.7 10
/10 R1AB_SARS2 Non-structural protein 3

7jir[1] B TTT
5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]be.. A 100.0
/99.7 11
/11 R1A_SARS2 Papain-like protease

7cyq[1] L GDP
GUANOSINE-5'-DIPHOSPHATE[28 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 RNA-directed RNA polymerase

7d4f[1] G H3U
8-(3-(3-aminobenzamido)-4-methylbenzamido)naphthal.. D 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

7d4f[1] H H3U
8-(3-(3-aminobenzamido)-4-methylbenzamido)naphthal.. D 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

7dfg[1] G 1RP
6-fluoro-3-oxo-4-(5-O-phosphono-beta-D-ribofuranos.. C 100.0
/100.0 7
/7 R1AB_SARS2 RNA-directed RNA polymerase

7dfh[1] N RVP
RIBAVIRIN MONOPHOSPHATE[20 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 RNA-directed RNA polymeras

7doi[2] O HCU
[(2R)-4-(2-azanyl-6-oxidanylidene-3H-purin-9-yl)-2.. A 100.0
/100.0 6
/6 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] J AT9
[[(2R,3R,4R,5R)-5-(2-azanyl-6-oxidanylidene-1H-pur.. A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] K AT9
[[(2R,3R,4R,5R)-5-(2-azanyl-6-oxidanylidene-1H-pur.. A 100.0
/100.0 11
/11 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] N AT9
[[(2R,3R,4R,5R)-5-(2-azanyl-6-oxidanylidene-1H-pur.. A 100.0
/100.0 6
/6 R1AB_SARS2 RNA-directed RNA polymerase

7jn2[1] B Y41
3-amino-2-methyl-N-[(1R)-1-(naphthalen-1-yl)ethyl].. A 100.0
/100.0 9
/9 R1A_SARS2 Papain-like protease

7k1l[6] C UVC
URIDINE-2',3'-VANADATE[21 atoms] A 100.0
/100.0 13
/13 R1AB_SARS2 Uridylate-specific endoribonuclease

7k1o[6] D VQV
1-(3,5-di-O-phosphono-alpha-L-xylofuranosyl)pyrimi.. A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

7keh[6] C B3P
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PR.. A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

7keh[3] E B3P
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PR.. B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7lbr[2] F XT7
5-[(azetidin-3-yl)amino]-N-[(1R)-1-{3-[5-({[(1S,3R.. A 100.0
/100.0 11
/11 R1A_SARS2 Non-structural protein 3

7lbs[2] C XR8
5-[(azetidin-3-yl)amino]-2-methyl-N-[(1R)-1-(3-{5-.. A 100.0
/100.0 12
/12 R1A_SARS2 Non-structural protein 3

7llf[2] I Y54
5-[(azetidin-3-yl)amino]-N-[(1R)-1-{3-[5-({[(1R,3S.. A 100.0
/100.0 11
/11 R1A_SARS2 Non-structural protein 3

7llz[2] C Y61
N-[(1R)-1-(3-{5-[(acetylamino)methyl]thiophen-2-yl.. A 100.0
/100.0 11
/11 R1A_SARS2 Non-structural protein 3

7los[2] E Y97
5-(azetidin-3-ylamino)-2-methyl-~{N}-[(1~{R})-1-[3.. A 100.0
/100.0 11
/11 R1A_SARS2 Non-structural protein 3

7n7r[3] C S6V
1-[2-(2-oxidanylidenepyrrolidin-1-yl)ethyl]-3-phen.. B 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

7n7u[6] C 0MI
1-[(2~{R},4~{S},5~{R})-5-[[(azanylidene-$l^{4}-aza.. A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

7n7u[6] C 0MI
1-[(2~{R},4~{S},5~{R})-5-[[(azanylidene-$l^{4}-aza.. A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7n7w[3] C 0OI
N-(2-fluorophenyl)-N'-methylurea[12 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

7n7y[6] C RZG
methyl 4-sulfamoylbenzoate[14 atoms] A 100.0
/100.0 14
/14 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[6] D WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[6] D WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[6] E WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[6] E WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[6] F WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

7n83[3] G WNM
(3S)-1-(phenylsulfonyl)pyrrolidin-3-amine[15 atoms.. A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

7nn0[4] E ANP
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER[31 ato.. A 100.0
/100.0 16
/16 R1AB_SARS2 SARS-CoV-2 helicase NSP13

7nng[2] C UJK
1-(2-methylphenyl)-1,2,3-triazole-4-carboxylic aci.. A 100.0
/100.0 8
/8 R1AB_SARS2 SARS-CoV-2 helicase NSP13

7nt4[1] M PRL
PROFLAVIN[16 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Non-structural protein 3

7nt4[2] N PRL
PROFLAVIN[16 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Non-structural protein 3

7ofs[1] E YRL
4-(2-hydroxyethyl)phenol[10 atoms] A 100.0
/100.0 10
/10 R1A_SARS2 Papain-like protease nsp3

7oft[1] K HBA
P-HYDROXYBENZALDEHYDE[9 atoms] A 100.0
/100.0 9
/9 R1A_SARS2 Papain-like protease nsp3

7ofu[1] B HE9
methyl 3,4-bis(oxidanyl)benzoate[12 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7qcg[1] B DZI
3,4,5-tris(oxidanyl)-N-[(E)-1H-pyrrol-2-ylmethylid.. A 100.0
/100.0 7
/7 R1A_SARS2 Papain-like protease nsp3

7qch[1] B A5I
N-(3,5-dimetoxy-4-hydroxybenzyliden)thiosemicarbaz.. A 100.0
/100.0 10
/10 R1A_SARS2 Papain-like protease nsp3

7qci[1] B A6Q
N-(3,4-dihydroxybenzylidene)-thiosemicarbazone[16 .. A 100.0
/100.0 10
/10 R1A_SARS2 Papain-like protease nsp3

7qcj[1] F A4O
N-(2,4-dihydroxybenzylidene)-thiosemicarbazone[14 .. A 100.0
/100.0 10
/10 R1A_SARS2 Papain-like protease nsp3

7qck[1] B A7L
N-(2,5-dihydroxybenzylidene)-thiosemicarbazone[16 .. A 100.0
/100.0 9
/9 R1A_SARS2 Papain-like protease nsp3

7qif[1] B GTG
7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE[52.. A 100.0
/100.0 14
/14 R1AB_SARS2 Proofreading exoribonuclease nsp14

7sdr[2] D JW9
4-({methyl[(1R)-1-(naphthalen-1-yl)ethyl]amino}met.. A 100.0
/100.0 12
/12 R1A_SARS2 Non-structural protein 3

7sgw[1] B L30
N-(naphthalen-1-yl)pyridine-3-carboxamide[19 atoms.. A 100.0
/100.0 9
/9 R1A_SARS2 Non-structural protein 3

7uo4[1] G NWX
[[(2~{R},3~{S},4~{R},5~{R})-5-(4-azanylpyrrolo[2,1.. A 100.0
/100.0 17
/17 R1AB_SARS2 RNA-directed RNA polymerase

7uo7[1] G ATP
ADENOSINE-5'-TRIPHOSPHATE[31 atoms] A 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase

7uo9[1] J UTP
URIDINE 5'-TRIPHOSPHATE [29 atoms] A 100.0
/100.0 12
/12 R1AB_SARS2 RNA-directed RNA polymerase

7uob[1] L GTP
GUANOSINE-5'-TRIPHOSPHATE[32 atoms] A 100.0
/100.0 16
/16 R1AB_SARS2 RNA-directed RNA polymerase

7uob[4] M GTP
GUANOSINE-5'-TRIPHOSPHATE[32 atoms] A 100.0
/100.0 19
/19 R1AB_SARS2 RNA-directed RNA polymerase

7uob[2] N L2B
3'-DEOXYURIDINE-5'-MONOPHOSPHATE[19 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 RNA-directed RNA polymerase

7uoe[1] K CTP
CYTIDINE-5'-TRIPHOSPHATE[29 atoms] A 100.0
/100.0 14
/14 R1AB_SARS2 RNA-directed RNA polymerase

8g62[3] E YOO
3-methoxy-5-(1-methylpiperidin-4-yl)-N-[4-(pyrroli.. A 100.0
/100.0 10
/10 R1A_SARS2 Non-structural protein 3

8g62[1] F YOO
3-methoxy-5-(1-methylpiperidin-4-yl)-N-[4-(pyrroli.. A 100.0
/100.0 10
/10 R1A_SARS2 Non-structural protein 3

8g62[2] M YOO
3-methoxy-5-(1-methylpiperidin-4-yl)-N-[4-(pyrroli.. A 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

8gwe[3] M GNP
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER[32 ato.. A 100.0
/100.0 13
/13 R1AB_SARS2 RNA-directed RNA polymerase

7e35[1] D GYX
N-[(3-acetamidophenyl)methyl]-1-[(1R)-1-naphthalen.. B 100.0
/99.7 2
/2 R1AB_SARS2 Non-structural protein 3

7e35[1] F GYX
N-[(3-acetamidophenyl)methyl]-1-[(1R)-1-naphthalen.. B 100.0
/99.7 10
/10 R1AB_SARS2 Non-structural protein 3

7rzc[5] D JWX
(1R)-N-[(1H-indol-3-yl)methyl]-N-methyl-1-(naphtha.. A 100.0
/100.0 10
/10 R1A_SARS2 Non-structural protein 3

7jit[1] B Y95
5-[(carbamoylcarbamoyl)amino]-2-methyl-N-[(1R)-1-(.. A 100.0
/99.7 11
/11 R1A_SARS2 Papain-like protease

7m1y[1] C 9JT
N-phenyl-2-selanylbenzamide[16 atoms] A 100.0
/99.7 7
/7 R1A_SARS2 Papain-like protease

5c8s[4] K SAH
S-ADENOSYL-L-HOMOCYSTEINE[26 atoms] B 100.0
/94.9 14
/14 R1AB_CVHSA Guanine-N7 methyltransferase

7ybg[1] C MLA
MALONIC ACID[7 atoms] A 83.3
/99.1 6
/6 R1A_SARS2 Papain-like protease nsp3

5c8s[2] L G3A
GUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE[50 atoms.. B 100.0
/94.9 16
/16 R1AB_CVHSA Guanine-N7 methyltransferase

5c8t[2] K SAM
S-ADENOSYLMETHIONINE[27 atoms] B 100.0
/94.9 13
/13 R1AB_CVHSA Guanine-N7 methyltransferase

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

METAL

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

5c8s[13] G ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5c8s[13] H ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5c8s[13] I ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5c8t[4] G ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5c8t[4] H ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5c8t[4] I ZN
ZINC ION[1 atoms] B 100.0
/94.9 4
/4 R1AB_CVHSA Guanine-N7 methyltransferase

5nfy[4] I ZN
ZINC ION[1 atoms] A 100.0
/94.7 5
/5 Q1T6X8_CVHSA Polyprotein 1ab

5nfy[4] J ZN
ZINC ION[1 atoms] A 100.0
/94.7 4
/4 Q1T6X8_CVHSA Polyprotein 1ab

5nfy[4] K ZN
ZINC ION[1 atoms] A 100.0
/94.7 5
/5 Q1T6X8_CVHSA Polyprotein 1ab

5rl6[144] C ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rl6[132] D ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5rl6[132] E ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

5skw[63] E ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

5skw[62] F ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

5skw[62] G ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5wwp[11] C ZN
ZINC ION[1 atoms] A 100.0
/72.3 4
/4 K0BWD0_9BETC ORF1ab

5wwp[14] D ZN
ZINC ION[1 atoms] A 100.0
/72.3 4
/4 K0BWD0_9BETC ORF1ab

6nur[4] E ZN
ZINC ION[1 atoms] A 100.0
/97.0 4
/4 R1AB_CVHSA NSP12

6nur[4] F ZN
ZINC ION[1 atoms] A 100.0
/97.0 4
/4 R1AB_CVHSA NSP12

6wrh[36] B ZN
ZINC ION[1 atoms] A 100.0
/99.7 4
/4 R1AB_SARS2 Non-structural protein 3

6wuu[19] I ZN
ZINC ION[1 atoms] A 100.0
/99.7 4
/4 R1AB_SARS2 Non-structural protein 3

6xez[37] I ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

6xez[37] J ZN
ZINC ION[1 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 RNA-directed RNA polymerase

6xez[20] O ZN
ZINC ION[1 atoms] E 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

6xez[25] P ZN
ZINC ION[1 atoms] E 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

6xez[20] Q ZN
ZINC ION[1 atoms] E 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

6xqb[8] G ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 RNA-directed RNA polymerase

6xqb[8] H ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

6yyt[6] I ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 nsp12

6yyt[6] J ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 nsp12

7bw4[1] E ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

7bw4[1] F ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 RNA-directed RNA polymerase

7cjm[1] C ZN
ZINC ION[1 atoms] A 100.0
/99.7 1
/1 R1AB_SARS2 Non-structural protein 3

7cjm[1] D ZN
ZINC ION[1 atoms] A 100.0
/99.7 2
/2 R1AB_SARS2 Non-structural protein 3

7d6h[4] B ZN
ZINC ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7ed5[1] G ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] H ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 RNA-directed RNA polymerase

7fac[1] C ZN
ZINC ION[1 atoms] A 100.0
/65.3 7
/7 R1A_SARS Non-structural protein 2

7jir[3] E ZN
ZINC ION[1 atoms] A 100.0
/99.7 2
/2 R1A_SARS2 Papain-like protease

7msw[2] B ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Non-structural protein 2

7r2v[1] I ZN
ZINC ION[1 atoms] A 100.0
/99.5 2
/2 R1AB_SARS2 Proofreading exoribonuclease nsp14

7r2v[2] J ZN
ZINC ION[1 atoms] A 100.0
/99.5 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

8g6r[1] F ZN
ZINC ION[1 atoms] A 100.0
/60.9 4
/4 A0A0U2C263_9ALPC nsp12

8g6r[1] G ZN
ZINC ION[1 atoms] A 100.0
/60.9 4
/4 A0A0U2C263_9ALPC nsp12

5c8s[16] J MG
MAGNESIUM ION[1 atoms] B 100.0
/94.9 3
/3 R1AB_CVHSA Guanine-N7 methyltransferase

6vww[3] E MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

6wuu[1] K MG
MAGNESIUM ION[1 atoms] B 100.0
/98.8 1
/1 R1AB_SARS2 Non-structural protein 3

6wuu[1] M MG
MAGNESIUM ION[1 atoms] C 100.0
/99.7 1
/1 R1AB_SARS2 Non-structural protein 3

6wuu[1] O MG
MAGNESIUM ION[1 atoms] D 100.0
/99.7 5
/5 R1AB_SARS2 Non-structural protein 3

6wuu[1] P MG
MAGNESIUM ION[1 atoms] D 100.0
/99.7 2
/2 R1AB_SARS2 Non-structural protein 3

6xez[22] K MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 RNA-directed RNA polymerase

6xez[19] T MG
MAGNESIUM ION[1 atoms] E 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

6xqb[20] I MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[2] I MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 2
/2 R1AB_SARS2 RNA-directed RNA polymerase

7ed5[1] L MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

7egq[2] HA MG
MAGNESIUM ION[1 atoms] H 100.0
/100.0 4
/4 R1AB_SARS2 Proofreading exoribonuclease

8gwe[1] T MG
MAGNESIUM ION[1 atoms] A 100.0
/100.0 2
/2 R1AB_SARS2 RNA-directed RNA polymerase

6vww[3] L CL
CHLORIDE ION[1 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6wrh[22] F CL
CHLORIDE ION[1 atoms] A 100.0
/99.7 3
/3 R1AB_SARS2 Non-structural protein 3

6wrh[7] G CL
CHLORIDE ION[1 atoms] A 100.0
/99.7 6
/6 R1AB_SARS2 Non-structural protein 3

7jir[6] H CL
CHLORIDE ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7jir[2] J CL
CHLORIDE ION[1 atoms] A 100.0
/99.7 3
/3 R1A_SARS2 Papain-like protease

7jn2[3] K CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Papain-like protease

7los[3] M CL
CHLORIDE ION[1 atoms] B 100.0
/100.0 1
/1 R1A_SARS2 Non-structural protein 3

7m1y[1] E CL
CHLORIDE ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7nfv[4] F CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Papain-like protease nsp3

7oft[1] E CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7oft[1] F CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7oft[1] H CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Papain-like protease nsp3

7oft[2] I CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7oft[1] J CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7qcj[3] L CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7qcj[1] N CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease nsp3

7qcm[1] J CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

8g62[3] I CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

6x4i[3] P NA
SODIUM ION[1 atoms] B 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7m1y[3] P NA
SODIUM ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7ybg[1] E NA
SODIUM ION[1 atoms] A 66.7
/99.1 3
/3 R1A_SARS2 Papain-like protease nsp3

7ybg[1] F NA
SODIUM ION[1 atoms] A 100.0
/99.1 4
/4 R1A_SARS2 Papain-like protease nsp3

8cx9[2] R NA
SODIUM ION[1 atoms] B 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7d47[1] D CA
CALCIUM ION[1 atoms] A 100.0
/99.7 1
/1 R1A_SARS2 Non-structural protein 3

7n0b[2] G CA
CALCIUM ION[1 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Proofreading exoribonuclease

7jn2[2] M UNX
UNKNOWN ATOM OR ION[1 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease

7oft[1] L K
POTASSIUM ION[1 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease nsp3

7oft[1] M K
POTASSIUM ION[1 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7thm[3] H MN
MANGANESE (II) ION[1 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 RNA-directed RNA polymerase

8cx9[1] N BR
BROMIDE ION[1 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

8cx9[1] P BR
BROMIDE ION[1 atoms] B 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

8cx9[1] Q BR
BROMIDE ION[1 atoms] B 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7m1y[1] G IOD
IODIDE ION[1 atoms] A 100.0
/99.7 3
/3 R1A_SARS2 Papain-like protease

7m1y[1] H IOD
IODIDE ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7m1y[1] I IOD
IODIDE ION[1 atoms] A 100.0
/99.7 1
/1 R1A_SARS2 Papain-like protease

7m1y[1] J IOD
IODIDE ION[1 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7m1y[1] K IOD
IODIDE ION[1 atoms] A 100.0
/99.7 1
/1 R1A_SARS2 Papain-like protease

7m1y[1] L IOD
IODIDE ION[1 atoms] A 100.0
/99.7 2
/2 R1A_SARS2 Papain-like protease

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

HOMO

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

6xez[18] F R1AB_SARS2 Helicase[596 aa] E 100.0
/100.0 4
/4 R1AB_SARS2 Helicase

6xez[8] E R1AB_SARS2 Helicase[596 aa] F 100.0
/100.0 5
/5 R1AB_SARS2 Helicase

7cxm[2] H R1AB_SARS2 Helicase[596 aa] I 100.0
/100.0 3
/3 R1AB_SARS2 Helicase

7cyq[10] G R1AB_SARS2 Helicase[585 aa] H 100.0
/100.0 1
/1 R1AB_SARS2 Helicase

7nio[2] B R1AB_SARS2 SARS-CoV-2 helicase NSP13[585 aa] A 100.0
/100.0 14
/14 R1AB_SARS2 SARS-CoV-2 helicase NSP13

7rdx[3] E R1AB_SARS2 Helicase[590 aa] F 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

7re0[1] F R1AB_SARS2 Helicase[590 aa] E 100.0
/100.0 6
/6 R1AB_SARS2 Helicase

7egq[2] I R1AB_SARS2 RNA-directed RNA polymerase[926 aa] A 100.0
/100.0 4
/4 R1AB_SARS2 RNA-directed RNA polymerase

7re3[2] J R1AB_SARS2 RNA-directed RNA polymerase[927 aa] A 100.0
/100.0 9
/9 R1AB_SARS2 RNA-directed RNA polymerase

7n0d[2] D R1AB_SARS2 Proofreading exoribonuclease[512 aa] B 100.0
/99.8 9
/9 R1AB_SARS2 Proofreading exoribonuclease

7n0d[4] K R1AB_SARS2 Proofreading exoribonuclease[512 aa] B 100.0
/99.8 14
/14 R1AB_SARS2 Proofreading exoribonuclease

7n0d[2] B R1AB_SARS2 Proofreading exoribonuclease[512 aa] D 100.0
/99.8 11
/11 R1AB_SARS2 Proofreading exoribonuclease

5s6x[292] A R1AB_SARS2 Uridylate-specific endoribonuclease[348 aa] A 100.0
/100.0 27
/27 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6x[202] A R1AB_SARS2 Uridylate-specific endoribonuclease[348 aa] A 100.0
/100.0 27
/27 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6x[280] B R1AB_SARS2 Uridylate-specific endoribonuclease[348 aa] A 100.0
/100.0 14
/15 R1AB_SARS2 Uridylate-specific endoribonuclease

5s6y[30] B R1AB_SARS2 Uridylate-specific endoribonuclease[348 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[54] A R1AB_SARS2 Uridylate-specific endoribonuclease[348 aa] A 100.0
/100.0 26
/26 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[12] B R1AB_SARS2 Uridylate-specific endoribonuclease[347 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7k0r[18] C R1AB_SARS2 Uridylate-specific endoribonuclease[345 aa] A 100.0
/100.0 20
/20 R1AB_SARS2 Uridylate-specific endoribonuclease

7k0r[4] F R1AB_SARS2 Uridylate-specific endoribonuclease[345 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7k9p[12] B R1AB_SARS2 Uridylate-specific endoribonuclease[349 aa] A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7me0[6] C R1AB_SARS2 Uridylate-specific endoribonuclease[347 aa] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7me0[12] E R1AB_SARS2 Uridylate-specific endoribonuclease[347 aa] A 100.0
/100.0 25
/25 R1AB_SARS2 Uridylate-specific endoribonuclease

7n06[6] B R1AB_SARS2 Uridylate-specific endoribonuclease[347 aa] A 100.0
/100.0 24
/24 R1AB_SARS2 Uridylate-specific endoribonuclease

7n06[6] C R1AB_SARS2 Uridylate-specific endoribonuclease[347 aa] A 100.0
/100.0 23
/23 R1AB_SARS2 Uridylate-specific endoribonuclease

8d34[6] B R1AB_SARS2 Uridylate-specific endoribonuclease nsp15[348 aa] A 100.0
/99.7 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] D R1AB_SARS2 Uridylate-specific endoribonuclease nsp15[271 aa] A 100.0
/99.7 12
/14 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] D R1AB_SARS2 Uridylate-specific endoribonuclease nsp15[271 aa] E 100.0
/99.7 21
/21 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7tj2[1] D R1AB_SARS2 Uridylate-specific endoribonuclease nsp15[271 aa] F 100.0
/99.7 25
/25 R1AB_SARS2 Uridylate-specific endoribonuclease nsp15

7e35[1] A R1AB_SARS2 Non-structural protein 3[287 aa] B 100.0
/99.7 21
/21 R1AB_SARS2 Non-structural protein 3

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

PRECIPITANT

7096 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

5rl6[216] F PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

5skw[71] C PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

5skw[62] D PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Proofreading exoribonuclease nsp14

6wrh[1] C PO4
PHOSPHATE ION[5 atoms] A 83.3
/99.7 6
/6 R1AB_SARS2 Non-structural protein 3

6wrh[2] D PO4
PHOSPHATE ION[5 atoms] A 100.0
/99.7 2
/2 R1AB_SARS2 Non-structural protein 3

6wrh[2] E PO4
PHOSPHATE ION[5 atoms] A 100.0
/99.7 5
/5 R1AB_SARS2 Non-structural protein 3

6wxc[12] D PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

7d6h[1] C PO4
PHOSPHATE ION[5 atoms] A 83.3
/99.7 6
/6 R1A_SARS2 Papain-like protease

7k0r[6] H PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

7keg[6] C PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

7ofu[3] G PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 5
/5 R1A_SARS2 Papain-like protease nsp3

7ofu[3] H PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7ofu[6] I PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease nsp3

7qch[3] G PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease nsp3

7qci[1] I PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease nsp3

7qcj[2] J PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Papain-like protease nsp3

7qcj[1] K PO4
PHOSPHATE ION[5 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Papain-like protease nsp3

5s6x[96] C CIT
CITRIC ACID[13 atoms] A 100.0
/100.0 11
/11 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[12] N CIT
CITRIC ACID[13 atoms] A 100.0
/100.0 9
/9 R1AB_SARS2 Uridylate-specific endoribonuclease

5wwp[1] F SO4
SULFATE ION[5 atoms] A 100.0
/72.3 5
/5 K0BWD0_9BETC ORF1ab

6wlc[3] L SO4
SULFATE ION[5 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

7jrn[1] E SO4
SULFATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Non-structural protein 3

7jrn[4] F SO4
SULFATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Non-structural protein 3

7jrn[10] I SO4
SULFATE ION[5 atoms] B 100.0
/100.0 3
/3 R1A_SARS2 Non-structural protein 3

7jrn[1] J SO4
SULFATE ION[5 atoms] B 100.0
/100.0 5
/5 R1A_SARS2 Non-structural protein 3

7k1l[6] G SO4
SULFATE ION[5 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7keh[6] D SO4
SULFATE ION[5 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

7lbr[10] D SO4
SULFATE ION[5 atoms] A 100.0
/100.0 5
/5 R1A_SARS2 Non-structural protein 3

7lbs[1] H SO4
SULFATE ION[5 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

7llf[2] H SO4
SULFATE ION[5 atoms] A 100.0
/100.0 1
/1 R1A_SARS2 Non-structural protein 3

7llz[1] G SO4
SULFATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Non-structural protein 3

7llz[2] L SO4
SULFATE ION[5 atoms] B 100.0
/100.0 5
/5 R1A_SARS2 Non-structural protein 3

7nt4[1] T SO4
SULFATE ION[5 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Non-structural protein 3

7nt4[1] U SO4
SULFATE ION[5 atoms] B 100.0
/100.0 2
/2 R1AB_SARS2 Non-structural protein 3

6vww[8] C GOL
GLYCEROL[6 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] C GOL
GLYCEROL[6 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[6] F GOL
GLYCEROL[6 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[6] G GOL
GLYCEROL[6 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] I GOL
GLYCEROL[6 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] N GOL
GLYCEROL[6 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6wrh[9] H GOL
GLYCEROL[6 atoms] A 100.0
/99.7 3
/3 R1AB_SARS2 Non-structural protein 3

6wrh[3] I GOL
GLYCEROL[6 atoms] A 100.0
/99.7 6
/6 R1AB_SARS2 Non-structural protein 3

6xa9[3] G GOL
GLYCEROL[6 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Non-structural protein 3

6xa9[2] H GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Non-structural protein 3

7lbr[1] G GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Non-structural protein 3

7lbr[2] L GOL
GLYCEROL[6 atoms] B 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

7lbs[1] M GOL
GLYCEROL[6 atoms] B 100.0
/100.0 6
/6 R1A_SARS2 Non-structural protein 3

7lbs[1] N GOL
GLYCEROL[6 atoms] B 100.0
/100.0 6
/6 R1A_SARS2 Non-structural protein 3

7nfv[2] C GOL
GLYCEROL[6 atoms] A 100.0
/100.0 6
/6 R1A_SARS2 Papain-like protease nsp3

7ofu[8] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 7
/7 R1A_SARS2 Papain-like protease nsp3

7qcg[1] C GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7qcj[3] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

7qcj[2] E GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Papain-like protease nsp3

6vww[3] H ACY
ACETIC ACID[4 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] O ACY
ACETIC ACID[4 atoms] B 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

6vww[3] P ACY
ACETIC ACID[4 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] F ACT
ACETATE ION[4 atoms] A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] Q ACT
ACETATE ION[4 atoms] B 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] S ACT
ACETATE ION[4 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[4] T ACT
ACETATE ION[4 atoms] B 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[6] C ACT
ACETATE ION[4 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[6] C ACT
ACETATE ION[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[3] K ACT
ACETATE ION[4 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

7jir[2] L ACT
ACETATE ION[4 atoms] A 85.7
/99.7 7
/7 R1A_SARS2 Papain-like protease

7jn2[1] L ACT
ACETATE ION[4 atoms] A 100.0
/100.0 2
/2 R1A_SARS2 Papain-like protease

7k1l[3] E ACT
ACETATE ION[4 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

8g62[3] J ACT
ACETATE ION[4 atoms] A 100.0
/100.0 3
/3 R1A_SARS2 Non-structural protein 3

8g62[2] K ACT
ACETATE ION[4 atoms] A 100.0
/100.0 6
/6 R1A_SARS2 Non-structural protein 3

8g62[1] L ACT
ACETATE ION[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

6xez[18] S AF3
ALUMINUM FLUORIDE[4 atoms] E 100.0
/100.0 7
/7 R1AB_SARS2 Helicase

7aap[2] K POP
PYROPHOSPHATE 2-[9 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Non-structural protein 12

7bv2[5] H POP
PYROPHOSPHATE 2-[9 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 RNA-directed RNA polymerase

7dfg[4] M POP
PYROPHOSPHATE 2-[9 atoms] C 100.0
/100.0 7
/7 R1AB_SARS2 RNA-directed RNA polymerase

7lbs[2] F BO3
BORIC ACID[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS2 Non-structural protein 3

7lbs[2] G BO3
BORIC ACID[4 atoms] A 100.0
/100.0 7
/7 R1A_SARS2 Non-structural protein 3

7lbs[1] I BO3
BORIC ACID[4 atoms] A 100.0
/100.0 10
/10 R1A_SARS2 Non-structural protein 3

7lbs[1] O BO3
BORIC ACID[4 atoms] B 100.0
/100.0 2
/2 R1A_SARS2 Non-structural protein 3

6w01[32] C EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[18] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[6] E EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[12] F EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[15] I EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[6] J EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[6] K EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[3] L EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[3] M EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[9] O EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[29] P EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[20] R EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[21] CA EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[4] S EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[9] T EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[3] V EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] J EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[12] K EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[3] H EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6x1b[3] G EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6x1b[3] H EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[12] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[3] G EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[3] G EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[6] I EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6x4i[3] X EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

7k1l[3] F EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7k1l[3] F EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

7nt4[1] R EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Non-structural protein 3

7rzc[7] H EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 12
/12 R1A_SARS2 Non-structural protein 3

6wlc[3] U FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] U FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] V FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[6] K FMT
FORMIC ACID[3 atoms] A 100.0
/100.0 2
/2 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[3] K FMT
FORMIC ACID[3 atoms] A 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[3] P FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 4
/4 R1AB_SARS2 Uridylate-specific endoribonuclease

6wxc[6] Q FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[3] F FMT
FORMIC ACID[3 atoms] A 100.0
/100.0 8
/8 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[3] G FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[3] I FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 5
/5 R1AB_SARS2 Uridylate-specific endoribonuclease

6xdh[3] M FMT
FORMIC ACID[3 atoms] B 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

7m1y[1] M FMT
FORMIC ACID[3 atoms] A 100.0
/99.7 3
/3 R1A_SARS2 Papain-like protease

7m1y[1] N FMT
FORMIC ACID[3 atoms] A 100.0
/99.7 3
/3 R1A_SARS2 Papain-like protease

7m1y[1] O FMT
FORMIC ACID[3 atoms] A 100.0
/99.7 4
/4 R1A_SARS2 Papain-like protease

7jir[2] K MES
2-(N-MORPHOLINO)-ETHANESULFONIC ACID[12 atoms] A 100.0
/99.7 3
/3 R1A_SARS2 Papain-like protease

6wlc[6] D TRS
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL[8 atoms] A 100.0
/100.0 3
/3 R1AB_SARS2 Uridylate-specific endoribonuclease

6wlc[3] N TRS
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL[8 atoms] B 100.0
/100.0 1
/1 R1AB_SARS2 Uridylate-specific endoribonuclease

7r2v[1] E TRS
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL[8 atoms] A 100.0
/99.5 2
/2 R1AB_SARS2 Proofreading exoribonuclease nsp14

5nfy[2] L PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/94.7 2
/2 Q1T6X8_CVHSA Polyprotein 1ab

6w01[3] G PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 7
/7 R1AB_SARS2 Uridylate-specific endoribonuclease

6w01[6] H PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 6
/6 R1AB_SARS2 Uridylate-specific endoribonuclease

7r2v[2] D PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/99.5 4
/4 R1AB_SARS2 Proofreading exoribonuclease nsp14

7r2v[1] K PEG
DI(HYDROXYETHYL)ETHER[7 atoms] B 100.0
/99.5 3
/3 R1AB_SARS2 Proofreading exoribonuclease nsp14

7r2v[1] N PEG
DI(HYDROXYETHYL)ETHER[7 atoms] B 100.0
/99.5 1
/1 R1AB_SARS2 Proofreading exoribonuclease nsp14

7ybg[1] B DTT
2,3-DIHYDROXY-1,4-DITHIOBUTANE[8 atoms] A 100.0
/99.1 9
/9 R1A_SARS2 Papain-like protease nsp3

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

MONOMER
7096
	pdb_id	a¹	identity[%]²	description
	8gwe	A	100.0	R1AB_SARS2 RNA-directed RNA polymerase
	7msw	A	100.0	R1AB_SARS2 Non-structural protein 2
	7egq	R	100.0	R1AB_SARS2 Helicase
	7egq	P	100.0	R1AB_SARS2 Proofreading exoribonuclease
	5s72	B	100.0	R1AB_SARS2 Uridylate-specific endoribonuclease
	6wuu	B	98.8	R1AB_SARS2 Non-structural protein 3
	1.a¹:asym_id for the homologue. 2.identity[%]²:sequence identity between the query and the homologue.

Contact Molecules for Homologous Proteins

Summary Bars[0.0 %]

UniProt Feature Tables [P0DTD1(R1AB_SARS2)]