Structure of PDB 1rgq Chain B

Receptor sequence

>1rgqB (length=186) [Search protein sequence]

QMGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATC
INGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPC
TCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA
GHAVGLFRAAVCTRGVTKAVDFIPVENLETTMRSGS

3D structure

PDB

1rgq Hepatitis C NS3 protease inhibition by peptidyl-alpha-ketoamide inhibitors: kinetic mechanism and structure.

Chain

Resolution

2.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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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.

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)
BS01	peptide	B	T7 Y9 Q11 Q12 T13 R14 C19 T22 S23 E33 E35 V36 I38 V39 S40 R65 T66 I67 A68	T7 Y9 Q11 Q12 T13 R14 C19 T22 S23 E33 E35 V36 I38 V39 S40 R65 T66 I67 A68
BS02	peptide	B	T7 Y9 Q11	T7 Y9 Q11
BS03	ZN	B	C100 C102 C148	C100 C102 C148
BS04	AKP	B	Q44 T45 H60 I135 L138 K139 G140 S142 R158 A159 A160 V161 C162	Q44 T45 H60 I135 L138 K139 G140 S142 R158 A159 A160 V161 C162

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

View graph for
Biological Process

External links

PDB	RCSB:1rgq, PDBe:1rgq, PDBj:1rgq
PDBsum	1rgq
PubMed	14984200
UniProt	P27958\|POLG_HCV77 Genome polyprotein

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