Structure of PDB 3gct Chain F

Receptor sequence
>3gctF (length=131) Species: 9913 (Bos taurus) [Search protein sequence]
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDV
VVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFS
QTVSAVCLPSASDDFAAGTTCVTTGWGLTRY
3D structure
PDB3gct 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.
ChainF
Resolution1.6 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 F I16 V23 S26 W27 P28 W29 Q116 A120 V121 C122 I1 V8 S11 W12 P13 W14 Q101 A105 V106 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:3gct, PDBe:3gct, PDBj:3gct
PDBsum3gct
PubMed1888717
UniProtP00766|CTRA_BOVIN Chymotrypsinogen A

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