Structure of PDB 2a4q Chain A Binding Site BS01

Receptor Information
>2a4q Chain A (length=181) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVAKAVDFIPVENLETTMRS
Ligand information
>2a4q Chain B (length=22) Species: 3052230 (Hepacivirus hominis) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
KGSVVIVGRIVLSGKPAIIPKK
Receptor-Ligand Complex Structure
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PDB2a4q Synthesis and Biological Activity of Macrocyclic Inhibitors of Hepatitis C Virus (HCV) NS3 Protease
Resolution2.45 Å
Binding residue
(original residue number in PDB)		T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 T19 S20 E30 E32 V33 I35 V36 S37 R62 T63 I64 A65 V107 R109
Binding residue
(residue number reindexed from 1)		T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 T19 S20 E30 E32 V33 I35 V36 S37 R62 T63 I64 A65 V107 R109
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 3.6.4.13: RNA helicase.
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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