Structure of PDB 5voj Chain A

Receptor sequence
>5vojA (length=198) [Search protein sequence]
MASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGE
VQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDL
VGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPI
SYLKGSSGGPLLCPAGHAVGIFRAAVSTRGVAKAVDFIPVESLETTMR
3D structure
PDB5voj Hepatitis C Virus NS3/4A Protease Inhibitors Incorporating Flexible P2 Quinoxalines Target Drug Resistant Viral Variants.
ChainA
Resolution1.799 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H1057 D1081 G1137 S1139
Catalytic site (residue number reindexed from 1) H75 D99 G155 S157
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 9H4 A Q1041 F1043 Y1056 H1057 V1078 D1081 L1135 K1136 G1137 S1139 F1154 R1155 A1156 A1157 Q59 F61 Y74 H75 V96 D99 L153 K154 G155 S157 F172 R173 A174 A175 MOAD: Ki=3.6nM
PDBbind-CN: -logKd/Ki=8.44,Ki=3.6nM
BS02 ZN A C1097 C1099 C1145 H1149 C115 C117 C163 H167
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

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Molecular Function
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Biological Process
External links
PDB RCSB:5voj, PDBe:5voj, PDBj:5voj
PDBsum5voj
PubMed28594175
UniProtP26664|POLG_HCV1 Genome polyprotein

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