Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Pancreatic trypsin inhibitor Kunitz domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I2, Kunitz, conserved site
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Pancreatic trypsin inhibitor and Trypsin-1 (preferred)
PDBe Complex ID:
PDB-CPX-133756 (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
Pancreatic trypsin inhibitor
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
