Contact Molecules for Homologous Proteins


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PID QueryLength Homolgous Sequence in PDB UniProt Query TITLE
4030711 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=Viral protein genome-linked nsp9 ; AltName: Full=Non-structural protein 9; Short=nsp9; AltName: Full=RNA-capping enzyme subunit nsp9;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; EC=2.7.7.50 ; 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="Viral protein genome-linked 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"
6015-6015 BINDING /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1"
6017-6017 BINDING /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2"
6116-6116 BINDING /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1"
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"
6193-6193 BINDING /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2"
6198-6198 BINDING /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2"
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"
6402-6402 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
7n83 A 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[60] 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[59] 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[38] 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[24] 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[10] 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[25] 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[26] 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[14] 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[2] G RL40_HUMAN Ubiquitin variant UbV.CV2.1[75 aa] A 100.0
/100.0
12
/12
R1A_SARS2 Papain-like protease nsp3
8cx9[2] H RL40_HUMAN Ubiquitin variant UbV.CV2.1[75 aa] A 100.0
/100.0
6
/6
R1A_SARS2 Papain-like protease nsp3
8iho[1] C covalent inhibitor[4 aa] A 100.0
/100.0
18
/18
R1A_SARS2 Papain-like protease nsp3
8iho[1] D covalent inhibitor[4 aa] A 100.0
/100.0
1
/1
R1A_SARS2 Papain-like protease nsp3
8sq9[1] E R1AB_SARS2 Non-structural protein 9[98 aa] A 100.0
/100.0
20
/20
R1AB_SARS2 RNA-directed RNA polymerase
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
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[2] C A0A0M4AW09_9ALPC nsp7[62 aa] A 81.2
/60.9
16
/16
A0A0U2C263_9ALPC nsp12
8urb[1] B U6BRU0_9ALPC nsp8[184 aa] A 54.3
/60.7
46
/47
U6BRU0_9ALPC nsp12
8urb[1] D U6BRU0_9ALPC nsp8[184 aa] A 66.7
/60.7
12
/12
U6BRU0_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[13] 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[2] H template A 100.0
/100.0
21
/21
R1AB_SARS2 RNA-directed RNA polymerase
8gwe[1] J template F 100.0
/100.0
1
/1
R1AB_SARS2 Helicase nsp13
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[2] 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
8gw1[1] F Template A 100.0
/99.9
23
/23
R1AB_SARS2 Replicase polyprotein 1ab
8gw1[1] F Template G 100.0
/100.0
1
/1
R1AB_SARS2 Helicase
8gwb[1] H RNA (5'-R(P*AP*U)-3') A 100.0
/100.0
9
/9
R1AB_SARS2 RNA-directed RNA polymerase
8gwb[6] J template A 100.0
/100.0
27
/27
R1AB_SARS2 RNA-directed RNA polymerase
8gwb[4] J template E 100.0
/100.0
5
/5
R1AB_SARS2 Helicase
8gwe[1] H RNA (5'-R(P*AP*UP*UP*A)-3') A 100.0
/100.0
15
/15
R1AB_SARS2 RNA-directed RNA polymerase
8sq9[1] F Primer RNA A 100.0
/100.0
14
/14
R1AB_SARS2 RNA-directed RNA polymerase
8sqj[1] F Primer RNA A 100.0
/100.0
12
/12
R1AB_SARS2 RNA-directed RNA polymerase
8sqj[1] G Template RNA A 100.0
/100.0
23
/23
R1AB_SARS2 RNA-directed RNA polymerase
8sqj[1] H SARS-CoV-2 5' UTR A 100.0
/100.0
18
/18
R1AB_SARS2 RNA-directed RNA polymerase
8sqk[1] F Primer RNA A 100.0
/100.0
12
/12
R1AB_SARS2 RNA-directed RNA polymerase nsp12
8sqk[1] G Template RNA A 100.0
/100.0
23
/23
R1AB_SARS2 RNA-directed RNA polymerase nsp12
8sqk[1] H SARS-CoV-2 5' UTR A 100.0
/100.0
8
/8
R1AB_SARS2 RNA-directed RNA polymerase nsp12
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
8urb[1] E RNA (33-MER) A 93.8
/60.7
16
/16
U6BRU0_9ALPC nsp12
8urb[1] F RNA (55-MER) A 76.2
/60.7
21
/21
U6BRU0_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
8gw1[2] T U5P
URIDINE-5'-MONOPHOSPHATE[20 atoms]
A 100.0
/99.9
8
/8
R1AB_SARS2 Replicase polyprotein 1ab
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
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
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
8gy6[1] E GO3
Gossypol[38 atoms]
A 100.0
/100.0
6
/6
R1AB_SARS2 RNA-directed RNA polymerase
8gy6[1] F GO3
Gossypol[38 atoms]
A 100.0
/100.0
5
/5
R1AB_SARS2 RNA-directed RNA polymerase
8sq9[1] L WSB
5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosph..
A 100.0
/100.0
15
/15
R1AB_SARS2 RNA-directed RNA polymerase
8sq9[1] O WSB
5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosph..
A 100.0
/100.0
12
/12
R1AB_SARS2 RNA-directed RNA polymerase
8sqj[2] I VSN
5'-O-[(R)-hydroxy(thiophosphonooxy)phosphoryl]guan..
A 100.0
/100.0
5
/5
R1AB_SARS2 RNA-directed RNA polymerase
8sqk[1] J VSN
5'-O-[(R)-hydroxy(thiophosphonooxy)phosphoryl]guan..
A 100.0
/100.0
17
/17
R1AB_SARS2 RNA-directed RNA polymerase nsp12
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[3] 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
5c8s[4] K SAH
S-ADENOSYL-L-HOMOCYSTEINE[26 atoms]
B 100.0
/94.9
14
/14
R1AB_CVHSA Guanine-N7 methyltransferase
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[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[26] 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[22] 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] N MG
MAGNESIUM ION[1 atoms]
A 100.0
/100.0
1
/1
R1AB_SARS2 RNA-directed RNA polymerase
6x4i[3] P NA
SODIUM ION[1 atoms]
B 100.0
/100.0
2
/2
R1AB_SARS2 Uridylate-specific endoribonuclease
8cx9[1] R NA
SODIUM ION[1 atoms]
B 100.0
/100.0
2
/2
R1A_SARS2 Papain-like protease nsp3
8g62[2] G NA
SODIUM ION[1 atoms]
A 100.0
/100.0
3
/3
R1A_SARS2 Non-structural protein 3
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
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[5] 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
6vww[3] L CL
CHLORIDE ION[1 atoms]
B 100.0
/100.0
3
/3
R1AB_SARS2 Uridylate-specific endoribonuclease
6wrh[20] F CL
CHLORIDE ION[1 atoms]
A 100.0
/99.7
3
/3
R1AB_SARS2 Non-structural protein 3
6wrh[3] G CL
CHLORIDE ION[1 atoms]
A 100.0
/99.7
6
/6
R1AB_SARS2 Non-structural protein 3
7los[6] M CL
CHLORIDE ION[1 atoms]
B 100.0
/100.0
1
/1
R1A_SARS2 Non-structural protein 3
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
7qcj[1] O CL
CHLORIDE ION[1 atoms]
A 100.0
/100.0
3
/3
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
7sqe[1] K CL
CHLORIDE ION[1 atoms]
B 75.0
/99.7
4
/4
R1A_SARS2 Papain-like protease
8g62[3] I CL
CHLORIDE ION[1 atoms]
A 100.0
/100.0
4
/4
R1A_SARS2 Non-structural protein 3
8u2x[3] E CL
CHLORIDE ION[1 atoms]
A 100.0
/99.7
2
/2
R1AB_SARS2 Uridylate-specific endoribonuclease nsp15
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[146] C ZN
ZINC ION[1 atoms]
A 100.0
/100.0
4
/4
R1AB_SARS2 Helicase
5rl6[134] D ZN
ZINC ION[1 atoms]
A 100.0
/100.0
4
/4
R1AB_SARS2 Helicase
5rl6[134] E ZN
ZINC ION[1 atoms]
A 100.0
/100.0
4
/4
R1AB_SARS2 Helicase
5skw[62] 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[11] 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[28] 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[41] I ZN
ZINC ION[1 atoms]
A 100.0
/100.0
4
/4
R1AB_SARS2 RNA-directed RNA polymerase
6xez[41] 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[22] 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[3] 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
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
8urb[1] G ZN
ZINC ION[1 atoms]
A 100.0
/60.7
4
/4
U6BRU0_9ALPC nsp12
8urb[1] H ZN
ZINC ION[1 atoms]
A 100.0
/60.7
4
/4
U6BRU0_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.
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[10] 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[9] 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
8gw1[1] H R1AB_SARS2 Helicase[585 aa] G 100.0
/100.0
1
/1
R1AB_SARS2 Helicase
7e35[2] A R1AB_SARS2 Non-structural protein 3[287 aa] B 100.0
/99.7
21
/21
R1AB_SARS2 Non-structural protein 3
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[295] 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[57] 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
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[2] 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[3] 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
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
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
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
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
8u2x[3] C TRS
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL[8 atoms]
A 100.0
/99.7
3
/3
R1AB_SARS2 Uridylate-specific endoribonuclease nsp15
6w01[31] 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[19] 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[5] H EDO
1,2-ETHANEDIOL[4 atoms]
A 100.0
/100.0
12
/12
R1A_SARS2 Non-structural protein 3
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
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.