Structure of PDB 2oin Chain B

Receptor sequence
>2oinB (length=181) [Search protein sequence]
APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFKAAVCTRGVAKAVDFIPVENLETTMRS
3D structure
PDB2oin Phenotypic and structural analyses of hepatitis C virus NS3 protease Arg155 variants: sensitivity to telaprevir (VX-950) and interferon alpha.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 peptide B T1030 Y1032 A1033 T4 Y6 A7
BS02 peptide B T1030 A1031 Y1032 A1033 Q1034 T1036 R1037 S1046 E1056 E1058 V1059 I1061 V1062 S1063 R1088 T1089 I1090 R1135 T4 A5 Y6 A7 Q8 T10 R11 S20 E30 E32 V33 I35 V36 S37 R62 T63 I64 R109
BS03 ZN B C1123 C1125 C97 C99
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
PDBsum2oin
PubMed17556358
UniProtP27958|POLG_HCV77 Genome polyprotein

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