Structure of PDB 2k1q Chain A

Receptor sequence
>2k1qA (length=165) [Search protein sequence]
TGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPI
TQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGD
SRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVP
VESMETTMRASKKKK
3D structure
PDB2k1q Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.
ChainA
ResolutionN/A
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) H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) H36 D60 G116 S118
Enzyme Commision number 3.4.21.98: hepacivirin.
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 Q41 S42 H57 G58 V132 L135 K136 G137 S139 A156 A157 Q20 S21 H36 G37 V111 L114 K115 G116 S118 A135 A136
BS02 ZN A C97 C99 C145 C76 C78 C124
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:2k1q, PDBe:2k1q, PDBj:2k1q
PDBsum2k1q
PubMed19061898
UniProtP90191

[Back to BioLiP]