Structure of PDB 1a1r Chain B

Receptor sequence
>1a1rB (length=179) [Search protein sequence]
PITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGV
CWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGS
SDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAV
GLFRAAVCTRGVAKAVDFIPVENLETTMR
3D structure
PDB1a1r Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H83 D107 G163 S165
Catalytic site (residue number reindexed from 1) H56 D80 G136 S138
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 B A31 Y32 A33 A4 Y5 A6
BS02 peptide B T30 A31 Y32 A33 Q34 Q35 T36 R37 C42 T45 S46 E56 E58 V59 I61 V62 S63 R88 T89 I90 A91 T3 A4 Y5 A6 Q7 Q8 T9 R10 C15 T18 S19 E29 E31 V32 I34 V35 S36 R61 T62 I63 A64
BS03 ZN B C123 C125 C171 C96 C98 C144
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:1a1r, PDBe:1a1r, PDBj:1a1r
PDBsum1a1r
PubMed8861917
UniProtP27958|POLG_HCV77 Genome polyprotein

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