Structure of PDB 1a1r Chain A

Receptor sequence
>1a1rA (length=152) [Search protein sequence]
VEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNV
DQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLS
PRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETT
MR
3D structure
PDB1a1r Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H83 D107 G163 S165
Catalytic site (residue number reindexed from 1) H29 D53 G109 S111
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 A V55 G57 E58 V59 Q60 I61 V62 S63 T89 I90 A91 P114 G116 V1 G3 E4 V5 Q6 I7 V8 S9 T35 I36 A37 P60 G62
BS02 ZN A C123 C125 C171 C69 C71 C117
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1a1r, PDBe:1a1r, PDBj:1a1r
PDBsum1a1r
PubMed8861917
UniProtP27958|POLG_HCV77 Genome polyprotein

[Back to BioLiP]