Structure of PDB 7mmd Chain A Binding Site BS02

Receptor Information
>7mmd Chain A (length=197) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGE
VQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDL
VGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPI
SYLKGSSGGPLLCPAGHAVGIFRAAVSTRGVAKAVAFIPVESLETTM
Ligand information
Ligand IDZJP
InChIInChI=1S/C38H50N6O9S/c1-23-33(40-30-19-26(51-3)15-16-28(30)39-23)52-27-20-31-32(45)42-38(35(47)43-54(49,50)37(2)17-18-37)21-24(38)11-7-5-4-6-8-14-29(34(46)44(31)22-27)41-36(48)53-25-12-9-10-13-25/h7,11,15-16,19,24-25,27,29,31H,4-6,8-10,12-14,17-18,20-22H2,1-3H3,(H,41,48)(H,42,45)(H,43,47)/b11-7-/t24-,27-,29+,31+,38-/m1/s1
InChIKeyAWCLTDQQVULZEM-UIWVBJMMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7Cc1c(nc2cc(ccc2n1)OC)O[C@@H]3C[C@H]4C(=O)N[C@@]5(C[C@H]5/C=C\CCCCC[C@@H](C(=O)N4C3)NC(=O)OC6CCCC6)C(=O)NS(=O)(=O)C7(CC7)C
CACTVS 3.385COc1ccc2nc(C)c(O[CH]3C[CH]4N(C3)C(=O)[CH](CCCCCC=C[CH]5C[C]5(NC4=O)C(=O)N[S](=O)(=O)C6(C)CC6)NC(=O)OC7CCCC7)nc2c1
CACTVS 3.385COc1ccc2nc(C)c(O[C@@H]3C[C@@H]4N(C3)C(=O)[C@H](CCCCC\C=C/[C@@H]5C[C@]5(NC4=O)C(=O)N[S](=O)(=O)C6(C)CC6)NC(=O)OC7CCCC7)nc2c1
OpenEye OEToolkits 2.0.7Cc1c(nc2cc(ccc2n1)OC)OC3CC4C(=O)NC5(CC5C=CCCCCCC(C(=O)N4C3)NC(=O)OC6CCCC6)C(=O)NS(=O)(=O)C7(CC7)C
ACDLabs 12.01CC1(CC1)S(=O)(=O)NC(=O)C12NC(=O)C3CC(Oc4nc5cc(OC)ccc5nc4C)CN3C(=O)C(NC(=O)OC3CCCC3)CCCCCC=CC2C1
FormulaC38 H50 N6 O9 S
Namecyclopentyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate
ChEMBLCHEMBL4076862
DrugBank
ZINC
PDB chain7mmd Chain A Residue 1206 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7mmd Deciphering the Molecular Mechanism of HCV Protease Inhibitor Fluorination as a General Approach to Avoid Drug Resistance.
Resolution1.89 Å
Binding residue
(original residue number in PDB)		Q1041 F1043 Y1056 H1057 V1078 D1081 R1123 L1135 K1136 G1137 S1139 F1154 R1155 A1156 A1157
Binding residue
(residue number reindexed from 1)		Q59 F61 Y74 H75 V96 D99 R141 L153 K154 G155 S157 F172 R173 A174 A175
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.7.48: RNA-directed RNA polymerase.
3.4.21.98: hepacivirin.
3.4.22.-
3.6.1.15: nucleoside-triphosphate phosphatase.
3.6.4.13: RNA helicase.
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7mmd, PDBe:7mmd, PDBj:7mmd
PDBsum7mmd
PubMed35183560
UniProtP26664|POLG_HCV1 Genome polyprotein

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