eF-site ID 6xoa-ABCD PDB Code 6xoa Chain A, B, C, D click to enlarge Title The crystal structure of 3CL MainPro of SARS-CoV-2 with C145S mutation Classification HYDROLASE Compound 3C-like proteinase Source (R1AB_SARS2) Sequence A:  SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPR HVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSFLNGSSGSVGFNIDYDCVSFC YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRT ILGSALLEDEFTPFDVVRQCSGVTFQ B:  SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPR HVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSFLNGSSGSVGFNIDYDCVSFC YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRT ILGSALLEDEFTPFDVVRQCSGVTFQ C:  SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPR HVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSFLNGSSGSVGFNIDYDCVSFC YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRT ILGSALLEDEFTPFDVVRQCSGVTFQ D:  SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPR HVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSFLNGSSGSVGFNIDYDCVSFC YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTI TVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRT ILGSALLEDEFTPFDVVRQCSGVTFQ Description Functional site 1) chain A residue 5 type sequence K description binding site for residue EDO A 401 source : AC1 2) chain A residue 127 type sequence Q description binding site for residue EDO A 401 source : AC1 3) chain B residue 5 type sequence K description binding site for residue EDO A 401 source : AC1 4) chain B residue 127 type sequence Q description binding site for residue EDO A 401 source : AC1 5) chain C residue 4 type sequence R description binding site for residue EDO C 401 source : AC2 6) chain C residue 5 type sequence K description binding site for residue EDO C 401 source : AC2 7) chain D residue 5 type sequence K description binding site for residue EDO C 401 source : AC2 8) chain C residue 5 type sequence K description binding site for residue EDO D 401 source : AC3 9) chain C residue 126 type sequence Y description binding site for residue EDO D 401 source : AC3 10) chain D residue 5 type sequence K description binding site for residue EDO D 401 source : AC3 11) chain D residue 126 type sequence Y description binding site for residue EDO D 401 source : AC3 12) chain D residue 127 type sequence Q description binding site for residue EDO D 401 source : AC3 13) chain A residue 41 type ACT_SITE sequence H description For 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000305|PubMed:32198291 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 41 type ACT_SITE sequence H description For 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000305|PubMed:32198291 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 41 type ACT_SITE sequence H description For 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000305|PubMed:32198291 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 41 type ACT_SITE sequence H description For 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000305|PubMed:32198291 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 145 type ACT_SITE sequence S description Nucleophile; for 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 145 type ACT_SITE sequence S description Nucleophile; for 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 145 type ACT_SITE sequence S description Nucleophile; for 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291 source Swiss-Prot : SWS_FT_FI2 20) chain D residue 145 type ACT_SITE sequence S description Nucleophile; for 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 306 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 306 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI3 23) chain C residue 306 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 306 type SITE sequence Q description Cleavage; by 3CL-PRO => ECO:0000250|UniProtKB:P0C6V3 source Swiss-Prot : SWS_FT_FI3

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