Structure of PDB 4u01 Chain G

Receptor sequence

>4u01G (length=182) Species: 333284 (Hepatitis C virus (isolate Con1)) [Search protein sequence]

APITAYSQQTRGLLGCIITSLTGRDRNQVEGEVQVVSTATQSFLATCVNG
VCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHA
VGIFRAAVCTRGVAKAVDFVPVESMETTMRAS

3D structure

PDB

4u01 Discovery and structural diversity of the hepatitis C virus NS3/4A serine protease inhibitor series leading to clinical candidate IDX320.

Chain

Resolution

2.8 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	G	T4 A5 Y6 S7 Q8 T10 R11 C16 T19 S20 E32 V33 Q34 V35 V36 S37 K62 T63 L64 A65	T4 A5 Y6 S7 Q8 T10 R11 C16 T19 S20 E32 V33 Q34 V35 V36 S37 K62 T63 L64 A65
BS02	39W	G	F43 Y56 H57 D81 V132 L135 K136 G137 S139 F154 R155 A156	F43 Y56 H57 D81 V132 L135 K136 G137 S139 F154 R155 A156

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:4u01, PDBe:4u01, PDBj:4u01
PDBsum	4u01
PubMed	26410074
UniProt	Q9WMX2\|POLG_HCVCO Genome polyprotein

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