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
- Proteinase inhibitor I11, ecotin
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I11, ecotin, gammaproteobacteria
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Ecotin and Anionic trypsin-2 (preferred)
PDBe Complex ID:
PDB-CPX-133402 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ecotin
Anionic trypsin-2
Molecule details ›
Chains: C, D
Length: 223 amino acids
Theoretical weight: 23.81 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.81 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
- Canonical:
P00763 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
