Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I3, Kunitz legume
- Serine proteases, trypsin domain
- Peptidase S1A, chymotrypsin family
- Peptidase S1, PA clan, chymotrypsin-like fold
- Kunitz inhibitor STI-like superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Trypsin and Trypsin inhibitor (preferred)
PDBe Complex ID:
PDB-CPX-123535 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 24.43 KDa
Source organism: Sus scrofa
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 231 amino acids
Theoretical weight: 24.43 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
P00761 (Residues: 1-231; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Trypsin inhibitor
Molecule details ›
Chain: B
Length: 185 amino acids
Theoretical weight: 20.6 KDa
Source organism: Tamarindus indica
UniProt:
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Length: 185 amino acids
Theoretical weight: 20.6 KDa
Source organism: Tamarindus indica
UniProt:
- Canonical: F4ZZG4 (Residues: 1-185; Coverage: 100%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)
