Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I12, Bowman-Birk
- Bowman-Birk type proteinase inhibitor
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Bowman-Birk type trypsin inhibitor and Trypsin (preferred)
PDBe Complex ID:
PDB-CPX-133394 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 23.46 KDa
Source organism: Sus scrofa
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.46 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
P00761 (Residues: 9-231; Coverage: 97%)
Structure domains: Trypsin-like serine proteases
Bowman-Birk type trypsin inhibitor
Molecule details ›
Chain: I
Length: 72 amino acids
Theoretical weight: 7.99 KDa
Source organism: Vigna radiata var. radiata
UniProt:
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Length: 72 amino acids
Theoretical weight: 7.99 KDa
Source organism: Vigna radiata var. radiata
UniProt:
- Canonical: P01062 (Residues: 1-72; Coverage: 100%)
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
