Structure of PDB 4i32 Chain B

Receptor sequence

>4i32B (length=182) Species: 11116 (Hepatitis C virus (isolate Japanese)) [Search protein sequence]

APITAYSQQTRGLLGCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNG
VCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSMTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHV
VGIFRAAVCTRGVAKAVVFIPVESMETTMRAS

3D structure

PDB

4i32 Molecular Mechanism by Which a Potent Hepatitis C Virus NS3-NS4A Protease Inhibitor Overcomes Emergence of Resistance.

Chain

Resolution

2.3001 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)	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	I3 T4 A5 Y6 S7 Q8 T10 R11 S20 D30 E32 V33 V35 L36 S37 K62 T63 L64 A65 R92 R109	I3 T4 A5 Y6 S7 Q8 T10 R11 S20 D30 E32 V33 V35 L36 S37 K62 T63 L64 A65 R92 R109
BS02	1BV	B	Q41 H57 D81 V132 L135 K136 G137 S139 F154 R155 A156 A157	Q41 H57 D81 V132 L135 K136 G137 S139 F154 R155 A156 A157

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:4i32, PDBe:4i32, PDBj:4i32
PDBsum	4i32
PubMed	23271737
UniProt	P26662\|POLG_HCVJA Genome polyprotein

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