Structure of PDB 2a4q Chain C

Receptor sequence
>2a4qC (length=151) [Search protein sequence]
VEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNV
DQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLS
PRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLETT
M
3D structure
PDB2a4q Synthesis and Biological Activity of Macrocyclic Inhibitors of Hepatitis C Virus (HCV) NS3 Protease
ChainC
Resolution2.45 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) H29 D53 G109 S111
Enzyme Commision number 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 C V29 G31 E32 V33 I35 V36 S37 R62 T63 I64 W85 P88 G90 V1 G3 E4 V5 I7 V8 S9 R34 T35 I36 W57 P60 G62
BS02 ZN C C97 C99 C145 C69 C71 C117
Gene Ontology
Molecular Function
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0019062 virion attachment to host cell
GO:0019087 transformation of host cell by virus
GO:0046718 symbiont entry into host cell
GO:0097264 self proteolysis
Cellular Component
GO:0016020 membrane
GO:0033644 host cell membrane
GO:0044423 virion component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2a4q, PDBe:2a4q, PDBj:2a4q
PDBsum2a4q
PubMed16112859
UniProtQ91RS4

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