Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I12, Bowman-Birk
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Bowman-Birk type proteinase inhibitor
- Peptidase S1, PA clan, chymotrypsin-like fold
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Bowman-Birk type trypsin inhibitor and Trypsin (preferred)
PDBe Complex ID:
PDB-CPX-133395 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chains: A, B, C, D
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.49 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 ›
Chains: I, J
Length: 125 amino acids
Theoretical weight: 13.93 KDa
Source organism: Hordeum vulgare
UniProt:
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
Length: 125 amino acids
Theoretical weight: 13.93 KDa
Source organism: Hordeum vulgare
UniProt:
- Canonical: P12940 (Residues: 1-41, 42-124; Coverage: 100%)
Sequence domains: Bowman-Birk serine protease inhibitor family
Structure domains: Cysteine Protease (Bromelain) Inhibitor, subunit H
