Structure of PDB 2gct Chain C Binding Site BS02
Receptor Information
>2gct Chain C (length=95) Species:
9913
(Bos taurus) [
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TPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLV
CKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
Ligand information
>2gct Chain D (length=4) [
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PGAY
Receptor-Ligand Complex Structure
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PDB
2gct
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.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
W172 K175 S190 C191 M192 G193 S195 V213 S214 W215 G216 S217
Binding residue
(residue number reindexed from 1)
W22 K25 S40 C41 M42 G43 S45 V63 S64 W65 G66 S67
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
PDBsum
2gct
PubMed
1888717
UniProt
P00766
|CTRA_BOVIN Chymotrypsinogen A
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