Structure of PDB 6bqj Chain B

Receptor sequence
>6bqjB (length=194) [Search protein sequence]
GSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGEVQIVSTA
TQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDLVGWQAPQ
GSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSS
GGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVESLETTMRSPA
3D structure
PDB6bqj Potent Inhibitors of Hepatitis C Virus NS3 Protease: Employment of a Difluoromethyl Group as a Hydrogen-Bond Donor.
ChainB
Resolution1.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) H68 D92 G148 S150
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 Z1B B Q41 Y56 H57 V78 D81 G137 S139 F154 R155 A156 A157 Q52 Y67 H68 V89 D92 G148 S150 F165 R166 A167 A168
BS02 ZN B C97 C99 C145 C108 C110 C156
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:6bqj, PDBe:6bqj, PDBj:6bqj
PDBsum6bqj
PubMed29456803
UniProtP27958|POLG_HCV77 Genome polyprotein

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