Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Elafin-like superfamily
- WAP-type 'four-disulfide core' domain
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assemblies composition:
Assembly name:
Trypsin and Antileukoproteinase (preferred)
PDBe Complex ID:
PDB-CPX-133383 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trypsin
Molecule details ›
Chains: A, C, E
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
UniProt:
- Canonical:
P00761 (Residues: 9-231; Coverage: 97%)
Structure domains: Trypsin-like serine proteases
Antileukoproteinase
Molecule details ›
Chains: B, D
Length: 47 amino acids
Theoretical weight: 5.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Sequence domains: WAP-type (Whey Acidic Protein) 'four-disulfide core'
Structure domains: Elafin-like
Length: 47 amino acids
Theoretical weight: 5.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P03973 (Residues: 85-131; Coverage: 44%)
Sequence domains: WAP-type (Whey Acidic Protein) 'four-disulfide core'
Structure domains: Elafin-like
