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BioLiP

Structure of PDB 2gct Chain C Binding Site BS01

Receptor Information
>2gct Chain C (length=95) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLV
CKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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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.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		Q157 S159 A206 W207
Binding residue
(residue number reindexed from 1)		Q7 S9 A56 W57
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.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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

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