Structure of PDB 2gct Chain C

Receptor sequence
>2gctC (length=95) Species: 9913 (Bos taurus) [Search protein sequence]
TPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLV
CKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
3D structure
PDB2gct Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.
ChainC
Resolution1.8 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) M192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) M42 G43 D44 S45 G46
Enzyme Commision number 3.4.21.1: chymotrypsin.
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 C Q157 S159 A206 W207 Q7 S9 A56 W57
BS02 peptide C W172 K175 S190 C191 M192 G193 S195 V213 S214 W215 G216 S217 W22 K25 S40 C41 M42 G43 S45 V63 S64 W65 G66 S67
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2gct, PDBe:2gct, PDBj:2gct
PDBsum2gct
PubMed1888717
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

[Back to BioLiP]