Structure of PDB 1rgq Chain A Binding Site BS01
Receptor Information
>1rgq Chain A (length=154) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTN
VDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLL
SPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVTKAVDFIPVENLET
TMRS
Ligand information
>1rgq Chain D (length=17) Species:
3052230
(Hepacivirus hominis) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
GSVVIVGRIVLSGKPAI
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1rgq
Hepatitis C NS3 protease inhibition by peptidyl-alpha-ketoamide inhibitors: kinetic mechanism and structure.
Resolution
2.9 Å
Binding residue
(original residue number in PDB)
V32 E35 V36 I38 V39 S40 R65 T66 I67 A68
Binding residue
(residue number reindexed from 1)
V2 E5 V6 I8 V9 S10 R35 T36 I37 A38
Enzymatic activity
Catalytic site (original residue number in PDB)
H60 D84 G140 S142
Catalytic site (residue number reindexed from 1)
H30 D54 G110 S112
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:1rgq
,
PDBe:1rgq
,
PDBj:1rgq
PDBsum
1rgq
PubMed
14984200
UniProt
P27958
|POLG_HCV77 Genome polyprotein
[
Back to BioLiP
]