Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I7, squash
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase/amylase inhibitor domain superfamily
- 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 dimer (preferred)
Assembly name:
Trypsin inhibitor 2 and Trypsin (preferred)
PDBe Complex ID:
PDB-CPX-133385 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chain: E
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
Trypsin inhibitor 2
Molecule details ›
Chain: I
Length: 36 amino acids
Theoretical weight: 3.9 KDa
Source organism: Ecballium elaterium
Expression system: Not provided
UniProt:
Length: 36 amino acids
Theoretical weight: 3.9 KDa
Source organism: Ecballium elaterium
Expression system: Not provided
UniProt:
- Canonical: P12071 (Residues: 1-30; Coverage: 100%)
