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
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I2, Kunitz, conserved site
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Trypsin-3 and Kunitz-type protease inhibitor 2 (preferred)
PDBe Complex ID:
PDB-CPX-128883 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kunitz-type protease inhibitor 2
Molecule details ›
Chain: X
Length: 55 amino acids
Theoretical weight: 6.3 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 55 amino acids
Theoretical weight: 6.3 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical:
O43291 (Residues: 34-88; Coverage: 24%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Trypsin-3
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 24.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 224 amino acids
Theoretical weight: 24.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P35030 (Residues: 81-304; Coverage: 74%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
