HOMCOS(prot_sch_conbars.cgi):

		Contact Molecules for Homologous Proteins
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PID

QueryLength

Homolgous Sequence in PDB

UniProt Query

TITLE

26061

4382

147

P0C6U8(R1A_SARS)

RecName: Full=Replicase polyprotein 1a; Short=pp1a;AltName: Full=ORF1a 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; Short=PL-PRO; EC=3.4.19.12 ; EC=3.4.22.- ; AltName: Full=Non-structural protein 3; Short=nsp3; AltName: Full=PL2-PRO;Contains: RecName: Full=Non-structural protein 4; Short=nsp4;Contains: RecName: Full=3C-like proteinase nsp5; Short=3CL-PRO; Short=3CLp; EC=3.4.22.69 ; AltName: Full=Main protease; Short=Mpro; AltName: Full=Non-structural protein 5; Short=nsp5; AltName: Full=SARS coronavirus main proteinase;Contains: RecName: Full=Non-structural protein 6; Short=nsp6;Contains: RecName: Full=Non-structural protein 7; Short=nsp7;Contains: RecName: Full=Non-structural protein 8; Short=nsp8;Contains: RecName: Full=RNA-capping enzyme subunit nsp9; AltName: Full=Non-structural protein 9; Short=nsp9; EC=2.7.7.50;Contains: RecName: Full=Non-structural protein 10; Short=nsp10; AltName: Full=Growth factor-like peptide; Short=GFL;Contains: RecName: Full=Non-structural protein 11; Short=nsp11;

QUERYSEQ

MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELG
TDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRI
RSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDL
LEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAY
VTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTV
LTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDE
WSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVA
GALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQK
PVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWN
LREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELG
VEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNN
CYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLC
ANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYR
HYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIA
THGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNS
SNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVEC
TTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLD
QALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSE
QLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTV
LRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDA
MNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFS
TFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIR
KSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYA
AVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAA
CAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITG
NTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQG
AVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVV
VPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGP
KVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVC
GMWKGYGCSCDQLREPLMQSADASTFLNGFAV

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

UniProt Feature Tables [P0C6U8(R1A_SARS)]

4382
	region	name	description
	1-4382	CHAIN	/note="Replicase polyprotein 1a" /id="PRO_0000338254"
	1-180	CHAIN	/note="Host translation inhibitor nsp1" /id="PRO_0000338255"
	181-818	CHAIN	/note="Non-structural protein 2" /id="PRO_0000338256"
	819-2740	CHAIN	/note="Papain-like protease nsp3" /id="PRO_0000338257"
	2741-3240	CHAIN	/note="Non-structural protein 4" /id="PRO_0000338258"
	3241-3546	CHAIN	/note="3C-like proteinase nsp5" /id="PRO_0000338259"
	3547-3836	CHAIN	/note="Non-structural protein 6" /id="PRO_0000338260"
	3837-3919	CHAIN	/note="Non-structural protein 7" /id="PRO_0000338261"
	3920-4117	CHAIN	/note="Non-structural protein 8" /id="PRO_0000338262"
	4118-4230	CHAIN	/note="RNA-capping enzyme subunit nsp9" /id="PRO_0000338263"
	4231-4369	CHAIN	/note="Non-structural protein 10" /id="PRO_0000338264"
	4370-4382	CHAIN	/note="Non-structural protein 11" /id="PRO_0000338265"
	1-2202	TOPO_DOM	/note="Cytoplasmic"
	2203-2223	TRANSMEM	/note="Helical"
	2224-2303	TOPO_DOM	/note="Lumenal"
	2304-2324	TRANSMEM	/note="Helical"
	2325-2754	TOPO_DOM	/note="Cytoplasmic"
	2755-2775	TRANSMEM	/note="Helical"
	2776-3021	TOPO_DOM	/note="Lumenal"
	3022-3042	TRANSMEM	/note="Helical"
	3043-3076	TOPO_DOM	/note="Cytoplasmic"
	3077-3097	TRANSMEM	/note="Helical"
	3098-3104	TOPO_DOM	/note="Lumenal"
	3105-3125	TRANSMEM	/note="Helical"
	3126-3563	TOPO_DOM	/note="Cytoplasmic"
	3564-3584	TRANSMEM	/note="Helical"
	3585-3585	TOPO_DOM	/note="Lumenal"
	3586-3606	TRANSMEM	/note="Helical"
	3607-3611	TOPO_DOM	/note="Cytoplasmic"
	3612-3632	TRANSMEM	/note="Helical"
	3633-3657	TOPO_DOM	/note="Lumenal"
	3658-3678	TRANSMEM	/note="Helical"
	3679-3727	TOPO_DOM	/note="Cytoplasmic"
	3728-3748	TRANSMEM	/note="Helical"
	3749-3755	TOPO_DOM	/note="Lumenal"
	3756-3776	TRANSMEM	/note="Helical"
	3777-4382	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"
	690-818	DOMAIN	/note="CoV Nsp2 C-terminal"
	822-930	DOMAIN	/note="Ubiquitin-like 1"
	1003-1169	DOMAIN	/note="Macro 1"
	1207-1335	DOMAIN	/note="Macro 2"
	1343-1470	DOMAIN	/note="Macro 3"
	1472-1538	DOMAIN	/note="DPUP"
	1542-1597	DOMAIN	/note="Ubiquitin-like 2"
	1611-1875	DOMAIN	/note="Peptidase C16"
	1888-1998	DOMAIN	/note="Nucleic acid-binding"
	2023-2132	DOMAIN	/note="G2M"
	2224-2294	DOMAIN	/note="3Ecto"
	2372-2740	DOMAIN	/note="CoV Nsp3 Y"
	3142-3240	DOMAIN	/note="Nsp4C"
	3241-3546	DOMAIN	/note="Peptidase C30"
	3837-3919	DOMAIN	/note="RdRp Nsp7 cofactor"
	3920-4117	DOMAIN	/note="RdRp Nsp8 cofactor"
	4118-4230	DOMAIN	/note="Nsp9 ssRNA-binding"
	4231-4369	DOMAIN	/note="ExoN/MTase coactivator"
	1729-1766	ZN_FING	/note="C4-type" ECO:0000269\|PubMed:16306590"
	4304-4320	ZN_FING
	4347-4360	ZN_FING
	200-236	REGION	/note="C2H2"
	323-344	REGION	/note="C4"
	370-416	REGION	/note="C2HC"
	972-1003	REGION	/note="Disordered"
	1175-1198	REGION	/note="Disordered"
	2203-2324	REGION	/note="HD1"
	2372-2462	REGION	/note="Y1"
	2376-2389	REGION	/note="ZF1"
	2422-2432	REGION	/note="ZF2"
	2463-2740	REGION	/note="CoV-Y"
	2463-2557	REGION	/note="Y2"
	2558-2639	REGION	/note="Y3"
	2640-2740	REGION	/note="Y4"
	2755-3125	REGION	/note="HD2"
	3564-3776	REGION	/note="HD3"
	972-997	COMPBIAS	/note="Acidic residues"
	1651-1651	ACT_SITE	/note="For PL-PRO activity"
	1812-1812	ACT_SITE	/note="For PL-PRO activity" ECO:0000269\|PubMed:16306590"
	1826-1826	ACT_SITE	/note="For PL-PRO activity" ECO:0000269\|PubMed:16306590"
	3281-3281	ACT_SITE	/note="For 3CL-PRO activity" ECO:0000269\|PubMed:16306590"
	3385-3385	ACT_SITE	/note="For 3CL-PRO activity"
	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"
	1729-1729	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	1732-1732	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	1764-1764	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	1766-1766	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4"
	2376-2376	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2381-2381	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2386-2386	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2389-2389	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="5"
	2422-2422	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	2425-2425	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	2429-2429	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	2432-2432	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="6"
	4304-4304	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4307-4307	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4313-4313	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4320-4320	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="7"
	4347-4347	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4350-4350	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4358-4358	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	4360-4360	BINDING	/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="8"
	1-4382	DISORDER	predicted by DISOPRED

MONOMER

4382

pdb_id a¹ identity[%]² description

7fac A 100.0 R1A_SARS Non-structural protein 2

4mm3 B 100.0 R1A_CVHSA Papain-like proteinase

7lmh A 100.0 R1A_SARS 3C-like proteinase

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

HETERO

4382 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1uk4[2] C 5-mer peptide of inhibitor[6 aa] A 100.0
/100.0 18
/18 R1AB_SARS 3C-like proteinase nsp5

1uk4[1] E 5-mer peptide of inhibitor[5 aa] B 100.0
/100.0 2
/2 R1AB_SARS 3C-like proteinase nsp5

2amq[2] C N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-.. A 100.0
/100.0 24
/24 R1AB_CVHSA 3C-like proteinase

2hob[10] B N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-.. A 100.0
/100.0 23
/23 R1AB_CVHSA Replicase polyprotein 1ab

3iwm[4] H N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-.. C 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

2z3c[4] B inhibitor[5 aa] A 100.0
/100.0 19
/19 R1AB_CVHSA Replicase polyprotein 1ab (pp1ab)

2z3d[2] B Inhibitor[5 aa] A 100.0
/100.0 18
/18 R1AB_CVHSA Replicase polyprotein 1ab (pp1ab)

3sna[2] B Peptide aldehyde inhibitor Ac-NSFSQ-H[6 aa] A 100.0
/100.0 17
/17 R1A_CVHSA 3C-like proteinase

3snb[2] B Peptide aldehyde inhibitor Ac-DSFDQ-H[6 aa] A 100.0
/100.0 19
/19 R1A_CVHSA 3C-like proteinase

3snc[2] B Peptide aldehyde inhibitor Ac-NSTSQ-H[6 aa] A 100.0
/100.0 18
/18 R1A_CVHSA 3C-like proteinase

3snd[2] C Peptide aldehyde inhibitor Ac-ESTLQ-H[2 aa] A 100.0
/100.0 12
/12 R1A_CVHSA 3C-like proteinase

3sne[2] B Peptide aldehyde inhibitor Ac-ESTLQ-H[6 aa] A 100.0
/100.0 21
/21 R1A_CVHSA 3C-like proteinase

3vb4[4] C B4Z inhibitor[5 aa] A 100.0
/100.0 21
/21 R1A_CVHSA 3C-like proteinase

3vb4[1] C B4Z inhibitor[5 aa] B 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

3vb6[2] C C6Z inhibitor[4 aa] A 100.0
/100.0 18
/18 R1A_CVHSA 3C-like proteinase

3vb6[1] D C6Z inhibitor[4 aa] A 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

3vb7[2] C M4Z inhibitor[4 aa] A 100.0
/100.0 20
/20 R1A_CVHSA 3C-like proteinase

3vb7[1] C M4Z inhibitor[4 aa] B 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

4mm3[2] A UBC_HUMAN Ubiquitin[76 aa] B 100.0
/100.0 25
/25 R1A_CVHSA Papain-like proteinase

5e6j[1] F UBB_HUMAN Polyubiquitin-B[75 aa] D 100.0
/100.0 10
/10 R1AB_CVHSA Replicase polyprotein 1ab

5tl6[2] D ISG15_HUMAN Ubiquitin-like protein ISG15[78 aa] A 100.0
/100.0 21
/21 R1AB_CVHSA Replicase polyprotein 1ab

5tl7[2] A ISG15_MOUSE Ubiquitin-like protein ISG15[77 aa] B 100.0
/100.0 27
/27 R1AB_CVHSA Replicase polyprotein 1ab

7lfu[3] B Papain-like protease peptide inhibitor VIR250[5 aa.. A 100.0
/100.0 16
/16 R1A_SARS papain-like protease

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

COMPOUND

4382 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1wof[2] C I12
N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]-L-ALANYL-L-VAL.. A 100.0
/100.0 23
/23 R1AB_CVHSA 3C-like proteinase

2a5i[6] B AZP
(5S,8S,14R)-ETHYL 11-(3-AMINO-3-OXOPROPYL)-8-BENZY.. A 100.0
/100.0 23
/23 R1AB_CVHSA 3C-like peptidase

2alv[2] B CY6
N-((3S,6R)-6-((S,E)-4-ETHOXYCARBONYL-1-((S)-2-OXOP.. A 100.0
/100.0 24
/24 R1AB_CVHSA Replicase polyprotein 1ab

2amd[2] C 9IN
N-(3-FUROYL)-D-VALYL-L-VALYL-N~1~-((1R,2Z)-4-ETHOX.. A 100.0
/100.0 23
/23 R1AB_CVHSA 3C-like proteinase

2d2d[2] C ENB
ETHYL (2E,4S)-4-[((2R)-2-{[N-(TERT-BUTOXYCARBONYL).. A 100.0
/100.0 21
/21 R1AB_CVHSA 3C-like proteinase

2gx4[2] B NOL
N-[(BENZYLOXY)CARBONYL]-O-(TERT-BUTYL)-L-THREONYL-.. A 100.0
/100.0 22
/22 R1AB_CVHSA 3C-like proteinase

2gx4[2] B NOL
N-[(BENZYLOXY)CARBONYL]-O-(TERT-BUTYL)-L-THREONYL-.. A 100.0
/100.0 1
/1 R1AB_CVHSA 3C-like proteinase

2gz7[2] B D3F
2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINI.. A 100.0
/100.0 13
/13 R1AB_CVHSA Replicase polyprotein 1ab

2gz8[2] B F3F
S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(P.. A 100.0
/100.0 14
/14 R1AB_CVHSA Replicase polyprotein 1ab

2op9[2] C WR1
NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-M.. A 100.0
/100.0 13
/13 R1AB_CVHSA Replicase polyprotein 1ab (pp1ab, ORF1AB) 3C-like ..

2v6n[2] B XP1
4-(DIMETHYLAMINO)BENZOIC ACID[11 atoms] A 100.0
/100.0 10
/10 R1AB_CVHSA REPLICASE POLYPROTEIN 1AB

2vj1[1] G XP1
4-(DIMETHYLAMINO)BENZOIC ACID[8 atoms] B 100.0
/100.0 6
/6 A7J8L3_CVHSA SARS CORONAVIRUS MAIN PROTEINASE

2vj1[1] D BEZ
BENZOIC ACID[9 atoms] A 100.0
/100.0 8
/8 A7J8L3_CVHSA SARS CORONAVIRUS MAIN PROTEINASE

2z94[2] C TLD
4-methylbenzene-1,2-dithiol[9 atoms] A 100.0
/100.0 3
/3 R1AB_CVHSA Replicase polyprotein 1ab

2zu4[2] B ZU3
N-[(benzyloxy)carbonyl]-3-[(2,2-dimethylpropanoyl).. A 100.0
/100.0 22
/22 R1A_CVHSA 3C-like proteinase

2zu4[2] B ZU3
N-[(benzyloxy)carbonyl]-3-[(2,2-dimethylpropanoyl).. A 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

2zu5[2] B ZU5
N-[(benzyloxy)carbonyl]-O-tert-butyl-L-threonyl-N-.. A 100.0
/100.0 22
/22 R1A_CVHSA 3C-like proteinase

2zu5[2] B ZU5
N-[(benzyloxy)carbonyl]-O-tert-butyl-L-threonyl-N-.. A 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

3d62[2] B 959
benzyl (2-oxopropyl)carbamate[15 atoms] A 100.0
/100.0 10
/10 R1AB_CVHSA 3C-like proteinase

3e9s[1] B TTT
5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]be.. A 100.0
/100.0 10
/10 R1A_CVHSA Non-structural protein 3

3mj5[1] C GRM
N-(1,3-benzodioxol-5-ylmethyl)-1-[(1R)-1-naphthale.. A 100.0
/100.0 9
/9 R1A_CVHSA Replicase polyprotein 1a

3mj5[1] E GRM
N-(1,3-benzodioxol-5-ylmethyl)-1-[(1R)-1-naphthale.. A 100.0
/100.0 4
/4 R1A_CVHSA Replicase polyprotein 1a

3sn8[2] B S89
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-Nalpha-[(2E.. A 100.0
/100.0 15
/15 R1A_CVHSA 3C-like proteinase

3szn[2] B G75
ETHYL (4R)-4-({N-[(BENZYLOXY)CARBONYL]-L-PHENYLALA.. A 100.0
/100.0 17
/17 R1A_CVHSA 3C-like proteinase

3tit[2] B G81
ETHYL (4R)-4-{[N-(TERT-BUTOXYCARBONYL)-L-PHENYLALA.. A 100.0
/100.0 15
/15 R1A_CVHSA SARS coronavirus main protease

3tiu[2] C G82
ETHYL (5S,8S,11R)-8-BENZYL-5-(3-TERT-BUTOXY-3-OXOP.. A 100.0
/100.0 23
/23 R1A_CVHSA SARS coronavirus main protease

3tns[2] B G83
ETHYL (5S,8S,11R)-8-BENZYL-5-(2-TERT-BUTOXY-2-OXOE.. A 100.0
/100.0 24
/24 R1A_CVHSA SARS coronavirus main protease

3tns[2] B G83
ETHYL (5S,8S,11R)-8-BENZYL-5-(2-TERT-BUTOXY-2-OXOE.. A 100.0
/100.0 1
/1 R1A_CVHSA SARS coronavirus main protease

3tnt[2] B G85
N-[(benzyloxy)carbonyl]-O-tert-butyl-L-seryl-N-{(2.. A 100.0
/100.0 22
/22 R1A_CVHSA SARS coronavirus main protease

3v3m[2] B 0EN
N-[(1R)-2-(tert-butylamino)-2-oxo-1-(pyridin-3-yl).. A 100.0
/100.0 15
/15 R1A_CVHSA 3C-like proteinase

4mds[2] B 23H
N-[4-(acetylamino)phenyl]-2-(1H-benzotriazol-1-yl).. A 100.0
/100.0 18
/18 R1A_CVHSA 3C-like proteinase

4ovz[1] D P85
N-[(4-fluorophenyl)methyl]-1-[(1R)-1-naphthalen-1-.. A 100.0
/100.0 11
/11 R1A_CVHSA Papain-like proteinase

4ow0[1] D S88
N-[(3-fluorophenyl)methyl]-1-[(1R)-1-naphthalen-1-.. A 100.0
/100.0 10
/10 R1A_CVHSA papain-like protease

5n19[2] B D03
(S)-N-benzyl-3-((S)-2-cinnamamido-3-phenylpropanam.. A 100.0
/100.0 21
/21 R1AB_CVHSA SARS coronavirus main protease

5n5o[2] B 8O5
(2~{R},3~{S})-3-[[(2~{S})-3-cyclopropyl-2-[[(~{E}).. A 100.0
/100.0 17
/17 R1AB_CVHSA Replicase polyprotein 1ab

6lnq[1] B EJF
N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxidanylidene.. A 100.0
/100.0 19
/19 Severe Acute Respiratory Syndrome Coronavirus 3c L..

6lny[1] B EOC
(2~{S})-4-methyl-~{N}-[(2~{S})-1-oxidanylidene-3-[.. A 100.0
/100.0 16
/16 R1A_CVHSA Replicase polyprotein 1a

6lo0[1] B EOF
(2~{S})-4-methyl-~{N}-[(2~{S})-1-oxidanylidene-3-[.. A 100.0
/100.0 18
/18 R1A_CVHSA Replicase polyprotein 1a

6w79[2] C X77
N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino).. A 100.0
/100.0 17
/17 Main protease

6wco[2] D X47
N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclopentylamino.. A 100.0
/100.0 17
/17 A0A3G5BIY8_CVHSA Main protease

6xhl[2] C V2M
N-[(2S)-1-({(2S,3S)-3,4-dihydroxy-1-[(3S)-2-oxopyr.. A 100.0
/100.0 18
/18 R1A_CVHSA 3C-like proteinase

6xhn[2] C V3D
(3S)-3-{[N-(4-methoxy-1H-indole-2-carbonyl)-L-leuc.. A 100.0
/100.0 17
/17 R1A_CVHSA 3C-like proteinase

6xho[2] D V34
ethyl (2E,4S)-4-{[N-(4-methoxy-1H-indole-2-carbony.. A 100.0
/100.0 19
/19 R1A_CVHSA 3C-like proteinase

6y7m[2] B OEW
~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclohexyl-1-[[(2.. A 100.0
/100.0 20
/20 R1A_SARS 3C-like proteinase

7end[2] B J7R
~{N}-[(1~{S},2~{R})-2-[[4-bromanyl-2-(methylcarbam.. A 100.0
/100.0 17
/17 R1A_CVHSA Replicase polyprotein 1a

7end[2] B J7R
~{N}-[(1~{S},2~{R})-2-[[4-bromanyl-2-(methylcarbam.. A 100.0
/100.0 1
/1 R1A_CVHSA Replicase polyprotein 1a

7eo8[1] C FNO
2-[(1R)-4-methyl-1-oxidanyl-pent-3-enyl]-5,8-bis(o.. A 100.0
/100.0 8
/8 R1A_CVHSA 3C-like proteinase

7k0h[2] E VR4
N-{(2S,3R)-4-(benzylamino)-3-hydroxy-4-oxo-1-[(3S).. A 100.0
/100.0 18
/18 R1A_CVHSA Replicase polyprotein 1a

7lcp[6] B UED
N~2~-[(benzyloxy)carbonyl]-N-{(2S)-1-hydroxy-3-[(3.. A 100.0
/100.0 14
/14 R1AB_SARS 3C-like proteinase

7lmg[2] C Y6G
2-(benzotriazol-1-yl)-~{N}-[4-(1~{H}-imidazol-4-yl.. A 100.0
/100.0 17
/17 R1A_SARS 3C-like proteinase

7lmh[2] B Y6D
2-(benzotriazol-1-yl)-~{N}-(4-pyridin-3-ylphenyl)-.. A 100.0
/100.0 19
/19 R1A_SARS 3C-like proteinase

7lmi[2] C Y6A
2-(benzotriazol-1-yl)-~{N}-[4-(1~{H}-pyrazol-4-yl).. A 100.0
/100.0 16
/16 R1A_SARS 3C-like proteinase

7lmj[2] E Y67
2-(benzotriazol-1-yl)-~{N}-[(3-chlorophenyl)methyl.. A 100.0
/100.0 18
/18 R1A_SARS 3C-like proteinase

7rc1[2] B 4IO
5-chloropyridin-3-yl 1-(3-nitrobenzene-1-sulfonyl).. A 100.0
/100.0 14
/14 R1A_SARS 3C-like proteinase

7vlo[2] C 4WI
(1R,2S,5S)-N-{(1E,2S)-1-imino-3-[(3S)-2-oxopyrroli.. A 100.0
/100.0 22
/22 R1A_SARS 3C-like proteinase

7wqi[2] C 80I
[(3~{S})-3-[[(2~{S})-2-[(4-methoxy-1~{H}-indol-2-y.. A 100.0
/100.0 14
/14 R1A_SARS 3C-like proteinase

7xax[1] C 3WL
5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one[20 atom.. A 100.0
/100.0 14
/14 R1A_SARS 3C-like proteinase nsp5

7ygq[2] C HUR
N-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-1-oxida.. A 100.0
/100.0 20
/20 R1A_SARS 3C-like proteinase nsp5

7zqw[2] B XNV
ethyl (4R)-4-({(2S)-2-[3-{[(5-methyl-1,2-oxazol-3-.. A 100.0
/100.0 19
/19 R1A_SARS 3C-like proteinase nsp5

8hus[2] C 7YY
6-[(6-chloranyl-2-methyl-indazol-5-yl)amino]-3-[(1.. A 100.0
/100.0 18
/18 R1A_SARS 3C-like proteinase nsp5

8uld[2] B WYR
N-[(benzyloxy)carbonyl]-4-fluoro-L-phenylalanyl-N-.. A 100.0
/100.0 19
/19 R1A_SARS Replicase polyprotein 1a

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

4382 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

2a5a[2] B CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1AB_CVHSA 3C-like peptidase

3e9s[1] D CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 R1A_CVHSA Non-structural protein 3

3e9s[1] E CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1A_CVHSA Non-structural protein 3

7k0h[1] C CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 3
/3 R1A_CVHSA Replicase polyprotein 1a

7k0h[1] D CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 1
/1 R1A_CVHSA Replicase polyprotein 1a

7lfv[1] FA CL
CHLORIDE ION[1 atoms] B 100.0
/100.0 1
/1 R1A_SARS papain-like protease

2fe8[14] D ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab

2z94[2] B ZN
ZINC ION[1 atoms] A 100.0
/100.0 2
/2 R1AB_CVHSA Replicase polyprotein 1ab

3e9s[1] C ZN
ZINC ION[1 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA Non-structural protein 3

5tl6[4] E ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab

7fac[1] B ZN
ZINC ION[1 atoms] A 100.0
/100.0 4
/4 R1A_SARS Non-structural protein 2

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

2fe8[6] E BR
BROMIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab

2fe8[6] F BR
BROMIDE ION[1 atoms] A 100.0
/100.0 3
/3 R1AB_CVHSA Replicase polyprotein 1ab

2fe8[6] G BR
BROMIDE ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab

2z9g[2] B HG
MERCURY (II) ION[1 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA 3C-like proteinase

5y3e[2] C NA
SODIUM ION[1 atoms] A 100.0
/100.0 4
/4 R1A_CVHSA Replicase polyprotein 1a

5y3e[2] D NA
SODIUM ION[1 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA Replicase polyprotein 1a

5y3e[2] E NA
SODIUM ION[1 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA Replicase polyprotein 1a

5y3e[2] F NA
SODIUM ION[1 atoms] A 100.0
/100.0 3
/3 R1A_CVHSA Replicase polyprotein 1a

5y3e[2] G NA
SODIUM ION[1 atoms] A 100.0
/100.0 7
/7 R1A_CVHSA Replicase polyprotein 1a

7lcp[2] D CA
CALCIUM ION[1 atoms] A 100.0
/100.0 3
/3 R1AB_SARS 3C-like proteinase

7lcp[2] E CA
CALCIUM ION[1 atoms] A 100.0
/100.0 3
/3 R1AB_SARS 3C-like proteinase

7lfv[1] DA NH4
AMMONIUM ION[1 atoms] B 100.0
/100.0 2
/2 R1A_SARS papain-like protease

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

HOMO

4382 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1q2w[170] B R1A_CVHSA 3C-like protease[297 aa] A 100.0
/100.0 26
/26 R1A_CVHSA 3C-like protease

2gtb[2] A R1AB_CVHSA 3C-like proteinase[299 aa] A 100.0
/100.0 2
/2 R1AB_CVHSA 3C-like proteinase

2z3e[2] A R1AB_CVHSA Replicase polyprotein 1ab (pp1ab)[306 aa] A 100.0
/100.0 5
/5 R1AB_CVHSA Replicase polyprotein 1ab (pp1ab)

3iwm[4] A R1A_CVHSA 3C-like proteinase[301 aa] A 100.0
/100.0 4
/4 R1A_CVHSA 3C-like proteinase

3iwm[8] B R1A_CVHSA 3C-like proteinase[301 aa] A 100.0
/100.0 1
/1 R1A_CVHSA 3C-like proteinase

3iwm[8] C R1A_CVHSA 3C-like proteinase[300 aa] A 100.0
/100.0 72
/72 R1A_CVHSA 3C-like proteinase

3iwm[8] D R1A_CVHSA 3C-like proteinase[300 aa] A 100.0
/100.0 3
/3 R1A_CVHSA 3C-like proteinase

3iwm[8] D R1A_CVHSA 3C-like proteinase[300 aa] A 100.0
/100.0 5
/5 R1A_CVHSA 3C-like proteinase

8uld[2] A R1A_SARS Replicase polyprotein 1a[305 aa] A 100.0
/100.0 31
/31 R1A_SARS Replicase polyprotein 1a

2fe8[6] B R1AB_CVHSA Replicase polyprotein 1ab[314 aa] A 100.0
/100.0 23
/23 R1AB_CVHSA Replicase polyprotein 1ab

2fe8[6] B R1AB_CVHSA Replicase polyprotein 1ab[314 aa] A 100.0
/100.0 8
/9 R1AB_CVHSA Replicase polyprotein 1ab

2fe8[7] C R1AB_CVHSA Replicase polyprotein 1ab[313 aa] A 100.0
/100.0 18
/18 R1AB_CVHSA Replicase polyprotein 1ab

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

4382 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1q2w[1] C MPD
(4S)-2-METHYL-2,4-PENTANEDIOL[8 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA 3C-like protease

2a5a[16] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA 3C-like peptidase

3vb3[1] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA 3C-like proteinase

3vb3[5] E EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_CVHSA 3C-like proteinase

3vb3[1] F EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA 3C-like proteinase

3vb3[3] G EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA 3C-like proteinase

3vb3[3] H EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA 3C-like proteinase

3vb3[1] I EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 3
/3 R1A_CVHSA 3C-like proteinase

3vb4[1] G EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 2
/2 R1A_CVHSA 3C-like proteinase

3vb4[2] J EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 2
/2 R1A_CVHSA 3C-like proteinase

3vb4[3] I EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 2
/2 R1A_CVHSA 3C-like proteinase

3vb4[1] L EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 5
/5 R1A_CVHSA 3C-like proteinase

3vb7[1] G EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 5
/5 R1A_CVHSA 3C-like proteinase

7lcp[4] C EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 2
/2 R1AB_SARS 3C-like proteinase

7lcq[2] B EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 7
/7 R1AB_SARS 3C-like proteinase

7lcq[2] C EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 1
/1 R1AB_SARS 3C-like proteinase

7lfv[1] F EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[1] G EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1A_SARS papain-like protease

7lfv[1] H EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[5] I EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1A_SARS papain-like protease

7lfv[1] J EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[1] K EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[1] L EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 3
/3 R1A_SARS papain-like protease

7lfv[1] M EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1A_SARS papain-like protease

7lfv[1] N EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[2] O EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[2] Q EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 5
/5 R1A_SARS papain-like protease

7lfv[1] BA EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 4
/4 R1A_SARS papain-like protease

7lfv[1] T EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 2
/2 R1A_SARS papain-like protease

7lfv[1] V EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 2
/2 R1A_SARS papain-like protease

7lfv[1] X EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 3
/3 R1A_SARS papain-like protease

7lfv[2] Y EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 3
/3 R1A_SARS papain-like protease

8uld[2] C EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/100.0 4
/4 R1A_SARS Replicase polyprotein 1a

2a5i[14] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA 3C-like peptidase

2z3e[2] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab (pp1ab)

3vb4[1] K GOL
GLYCEROL[6 atoms] B 100.0
/100.0 4
/4 R1A_CVHSA 3C-like proteinase

3vb7[1] H GOL
GLYCEROL[6 atoms] B 100.0
/100.0 6
/6 R1A_CVHSA 3C-like proteinase

4ow0[1] F GOL
GLYCEROL[6 atoms] A 100.0
/100.0 3
/3 R1A_CVHSA papain-like protease

5y3e[2] H GOL
GLYCEROL[6 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA Replicase polyprotein 1a

5y3e[2] I GOL
GLYCEROL[6 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA Replicase polyprotein 1a

5y3e[1] J GOL
GLYCEROL[6 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA Replicase polyprotein 1a

7lmg[8] B GOL
GLYCEROL[6 atoms] A 100.0
/100.0 8
/8 R1A_SARS 3C-like proteinase

7lmg[4] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 1
/1 R1A_SARS 3C-like proteinase

7lmh[6] D GOL
GLYCEROL[6 atoms] A 100.0
/100.0 6
/6 R1A_SARS 3C-like proteinase

2fe8[7] H SO4
SULFATE ION[5 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA Replicase polyprotein 1ab

2v6n[2] D SO4
SULFATE ION[5 atoms] A 100.0
/100.0 2
/2 R1AB_CVHSA REPLICASE POLYPROTEIN 1AB

5tl6[1] F SO4
SULFATE ION[5 atoms] A 100.0
/100.0 3
/3 R1AB_CVHSA Replicase polyprotein 1ab

7lfv[1] R SO4
SULFATE ION[5 atoms] A 100.0
/100.0 2
/2 R1A_SARS papain-like protease

7lfv[1] S SO4
SULFATE ION[5 atoms] A 100.0
/100.0 4
/4 R1A_SARS papain-like protease

2gt7[1] C MES
2-(N-MORPHOLINO)-ETHANESULFONIC ACID[12 atoms] B 100.0
/100.0 1
/1 R1AB_CVHSA 3C-like proteinase

2v6n[8] C MES
2-(N-MORPHOLINO)-ETHANESULFONIC ACID[12 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA REPLICASE POLYPROTEIN 1AB

6w79[4] E MES
2-(N-MORPHOLINO)-ETHANESULFONIC ACID[12 atoms] A 100.0
/100.0 3
/3 Main protease

2gtb[2] C ACY
ACETIC ACID[4 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA 3C-like proteinase

2vj1[1] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 1
/1 A7J8L3_CVHSA SARS CORONAVIRUS MAIN PROTEINASE

2vj1[2] E DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 3
/3 A7J8L3_CVHSA SARS CORONAVIRUS MAIN PROTEINASE

2vj1[1] F DMS
DIMETHYL SULFOXIDE[4 atoms] B 100.0
/100.0 3
/3 A7J8L3_CVHSA SARS CORONAVIRUS MAIN PROTEINASE

2z9j[6] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA 3C-like proteinase

2z9j[6] D DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 9
/9 R1AB_CVHSA 3C-like proteinase

2z9j[6] G DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 1
/1 R1AB_CVHSA 3C-like proteinase

3snc[14] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 2
/2 R1A_CVHSA 3C-like proteinase

3tiu[2] B DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA SARS coronavirus main protease

3v3m[4] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 8
/8 R1A_CVHSA 3C-like proteinase

4ovz[2] E DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 4
/4 R1A_CVHSA Papain-like proteinase

4ow0[1] G DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 5
/5 R1A_CVHSA papain-like protease

6y7m[2] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 5
/5 R1A_SARS 3C-like proteinase

7rc1[2] D DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 8
/8 R1A_SARS 3C-like proteinase

7rc1[2] E DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 5
/5 R1A_SARS 3C-like proteinase

7rc1[2] F DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 2
/2 R1A_SARS 3C-like proteinase

7rc1[2] G DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 3
/3 R1A_SARS 3C-like proteinase

7rc1[2] G DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/100.0 1
/1 R1A_SARS 3C-like proteinase

2z9g[2] C BNZ
BENZENE[6 atoms] A 100.0
/100.0 7
/7 R1AB_CVHSA 3C-like proteinase

2z9j[2] E DTZ
zinc(II)hydrogensulfide[3 atoms] A 100.0
/100.0 4
/4 R1AB_CVHSA 3C-like proteinase

2z9k[2] E DOZ
(dimethylamino)(hydroxy)zinc'[5 atoms] A 100.0
/100.0 5
/5 R1AB_CVHSA 3C-like proteinase

2z9l[2] E DAZ
diaminozinc[3 atoms] A 100.0
/100.0 2
/2 R1AB_CVHSA 3C-like proteinase

3snd[1] E MRD
(4R)-2-METHYLPENTANE-2,4-DIOL[8 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA 3C-like proteinase

3vb3[2] C PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 4
/4 R1A_CVHSA 3C-like proteinase

7lmg[4] E PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 2
/2 R1A_SARS 3C-like proteinase

7lmg[4] E PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 1
/1 R1A_SARS 3C-like proteinase

7lmj[2] G PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/100.0 3
/3 R1A_SARS 3C-like proteinase

5y3q[1] C BME
BETA-MERCAPTOETHANOL[4 atoms] A 100.0
/100.0 6
/6 R1A_CVHSA Replicase polyprotein 1a

7k0h[1] G PG4
TETRAETHYLENE GLYCOL[13 atoms] B 100.0
/100.0 10
/10 R1A_CVHSA Replicase polyprotein 1a

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

MONOMER
4382
	pdb_id	a¹	identity[%]²	description
	7fac	A	100.0	R1A_SARS Non-structural protein 2
	4mm3	B	100.0	R1A_CVHSA Papain-like proteinase
	7lmh	A	100.0	R1A_SARS 3C-like proteinase
	1.a¹:asym_id for the homologue. 2.identity[%]²:sequence identity between the query and the homologue.

Contact Molecules for Homologous Proteins

Summary Bars[100 %]

UniProt Feature Tables [P0C6U8(R1A_SARS)]