Structure of PDB 2obo Chain A Binding Site BS02

Receptor Information
>2obo Chain A (length=184) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCI
NGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCT
CGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAG
HAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSG
Ligand information
>2obo Chain D (length=17) Species: 31647 (Hepatitis C virus subtype 1b) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
KGSVVIVGRIVLSGKPA
Receptor-Ligand Complex Structure
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PDB2obo Discovery of the HCV NS3/4A protease inhibitor (1R,5S)-N-[3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl]-3- [2(S)-[[[(1,1-dimethylethyl)amino]carbonyl]amino]-3,3-dimethyl-1-oxobutyl]- 6,6-dimethyl-3-azabicyclo[3.1.0]hexan-2(S)-carboxamide (Sch 503034) II. Key steps in structure-based optimization.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		T4 Y6 A7
Binding residue
(residue number reindexed from 1)		T6 Y8 A9
Enzymatic activity
Catalytic site (original residue number in PDB) H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) H59 D83 G139 S141
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:2obo, PDBe:2obo, PDBj:2obo
PDBsum2obo
PubMed17444623
UniProtQ91RS4

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