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
- Peptidase S1A, chymotrypsin family
- Pacifastin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Pacifastin domain superfamily
- Protease inhibitor with pacifastin repeats
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133433 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymotrypsinogen A
Molecule details ›
Chains: A, B, C
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
Protease inhibitor LCMI-II
Molecule details ›
Chains: I, J, K
Length: 36 amino acids
Theoretical weight: 3.79 KDa
Source organism: Locusta migratoria
Expression system: Not provided
UniProt:
Length: 36 amino acids
Theoretical weight: 3.79 KDa
Source organism: Locusta migratoria
Expression system: Not provided
UniProt:
- Canonical: P80060 (Residues: 57-92; Coverage: 49%)
