Structure of PDB 1rgq Chain B Binding Site BS01

Receptor Information
>1rgq Chain B (length=186) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QMGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATC
INGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPC
TCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA
GHAVGLFRAAVCTRGVTKAVDFIPVENLETTMRSGS
Ligand information
>1rgq Chain C (length=22) Species: 3052230 (Hepacivirus hominis) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
KGSVVIVGRIVLSGKPAIIPKK
Receptor-Ligand Complex Structure
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PDB1rgq Hepatitis C NS3 protease inhibition by peptidyl-alpha-ketoamide inhibitors: kinetic mechanism and structure.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		T7 Y9 Q11 Q12 T13 R14 C19 T22 S23 E33 E35 V36 I38 V39 S40 R65 T66 I67 A68
Binding residue
(residue number reindexed from 1)		T7 Y9 Q11 Q12 T13 R14 C19 T22 S23 E33 E35 V36 I38 V39 S40 R65 T66 I67 A68
Enzymatic activity
Catalytic site (original residue number in PDB) H60 D84 G140 S142
Catalytic site (residue number reindexed from 1) H60 D84 G140 S142
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1rgq, PDBe:1rgq, PDBj:1rgq
PDBsum1rgq
PubMed14984200
UniProtP27958|POLG_HCV77 Genome polyprotein

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