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
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1
Molecule details ›
Chains: A, C
Length: 223 amino acids
Theoretical weight: 23.31 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.31 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Tissue factor pathway inhibitor 2
Molecule details ›
Chains: B, D
Length: 63 amino acids
Theoretical weight: 7.38 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: 63 amino acids
Theoretical weight: 7.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P48307 (Residues: 28-90; Coverage: 30%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
