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, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assemblies composition:
Assembly name:
Trypsin-3 and Pancreatic trypsin inhibitor (preferred)
PDBe Complex ID:
PDB-CPX-133755 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Pancreatic trypsin inhibitor
Molecule details ›
Chain: E
Length: 58 amino acids
Theoretical weight: 6.46 KDa
Source organism: Bos taurus
Expression system: Komagataella pastoris
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 58 amino acids
Theoretical weight: 6.46 KDa
Source organism: Bos taurus
Expression system: Komagataella pastoris
UniProt:
- Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
