Structure of PDB 2gct Chain B

Receptor sequence
>2gctB (length=131) Species: 9913 (Bos taurus) [Search protein sequence]
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDV
VVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFS
QTVSAVCLPSASDDFAAGTTCVTTGWGLTRY
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.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102
Catalytic site (residue number reindexed from 1) H42 D87
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 B I16 E20 V23 S26 W27 P28 Q116 A120 C122 I1 E5 V8 S11 W12 P13 Q101 A105 C107
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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