Structure of PDB 2oin Chain B Binding Site BS02
Receptor Information
>2oin Chain B (length=181) [
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APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFKAAVCTRGVAKAVDFIPVENLETTMRS
Ligand information
>2oin Chain D (length=21) Species:
32630
(synthetic construct) [
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KGSVVIVGRIVLSGKPAIIPA
Receptor-Ligand Complex Structure
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PDB
2oin
Phenotypic and structural analyses of hepatitis C virus NS3 protease Arg155 variants: sensitivity to telaprevir (VX-950) and interferon alpha.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
T1030 A1031 Y1032 A1033 Q1034 T1036 R1037 S1046 E1056 E1058 V1059 I1061 V1062 S1063 R1088 T1089 I1090 R1135
Binding residue
(residue number reindexed from 1)
T4 A5 Y6 A7 Q8 T10 R11 S20 E30 E32 V33 I35 V36 S37 R62 T63 I64 R109
Enzymatic activity
Catalytic site (original residue number in PDB)
H1083 D1107 G1163 S1165
Catalytic site (residue number reindexed from 1)
H57 D81 G137 S139
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:2oin
,
PDBe:2oin
,
PDBj:2oin
PDBsum
2oin
PubMed
17556358
UniProt
P27958
|POLG_HCV77 Genome polyprotein
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