Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
- not assigned
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 analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-524515 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S1 domain-containing protein
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 25.07 KDa
Source organism: Astacus leptodactylus
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 237 amino acids
Theoretical weight: 25.07 KDa
Source organism: Astacus leptodactylus
UniProt:
- Canonical:
Q52V24 (Residues: 1-237; Coverage: 100%)
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor
Molecule details ›
Chains: I, J
Length: 100 amino acids
Theoretical weight: 10.92 KDa
Source organism: Bos taurus
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 100 amino acids
Theoretical weight: 10.92 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00974 (Residues: 1-100; Coverage: 100%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
