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:
Trypsin and Tissue factor pathway inhibitor (preferred)
PDBe Complex ID:
PDB-CPX-133384 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
- Canonical:
P00761 (Residues: 9-231; Coverage: 97%)
Structure domains: Trypsin-like serine proteases
Tissue factor pathway inhibitor
Molecule details ›
Chains: C, D
Length: 58 amino acids
Theoretical weight: 6.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 58 amino acids
Theoretical weight: 6.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P10646 (Residues: 121-178; Coverage: 21%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
