Function and Biology Details
Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Serine proteases, trypsin domain
- Proteinase inhibitor I11, ecotin
- Peptidase S1A, chymotrypsin family
- Proteinase inhibitor I11, ecotin, gammaproteobacteria
- Peptidase S1, PA clan, chymotrypsin-like fold
- Ecotin superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Chymotrypsin A chain C and Ecotin (preferred)
PDBe Complex ID:
PDB-CPX-109321 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00766 (Residues: 1-245; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Ecotin
Molecule details ›
Chains: E, F, G, H
Length: 148 amino acids
Theoretical weight: 16.75 KDa
Source organism: Yersinia pseudotuberculosis YPIII
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Ecotin
Structure domains: Ecotin
Length: 148 amino acids
Theoretical weight: 16.75 KDa
Source organism: Yersinia pseudotuberculosis YPIII
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: B1JSA0 (Residues: 22-169; Coverage: 100%)
Sequence domains: Ecotin
Structure domains: Ecotin
