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 3 and Trypsin-1 (preferred)
PDBe Complex ID:
PDB-CPX-145264 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin-1
Molecule details ›
Chain: E
Length: 222 amino acids
Theoretical weight: 23.86 KDa
Source organism: Salmo salar
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 222 amino acids
Theoretical weight: 23.86 KDa
Source organism: Salmo salar
UniProt:
- Canonical:
P35031 (Residues: 21-242; Coverage: 98%)
Structure domains: Trypsin-like serine proteases
Trypsin inhibitor 3
Molecule details ›
Chain: I
Length: 29 amino acids
Theoretical weight: 3.27 KDa
Source organism: Cucurbita pepo
UniProt:
Length: 29 amino acids
Theoretical weight: 3.27 KDa
Source organism: Cucurbita pepo
UniProt:
- Canonical: P10293 (Residues: 4-32; Coverage: 91%)
