Function and Biology Details
Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I13, potato inhibitor I
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Proteinase inhibitor I13, potato inhibitor I superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Serine protease 1 and Proteinase inhibitor (preferred)
PDBe Complex ID:
PDB-CPX-133360 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1
Molecule details ›
Chains: A, B
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Proteinase inhibitor
Molecule details ›
Chains: C, D
Length: 79 amino acids
Theoretical weight: 9.02 KDa
Source organism: Fagopyrum esculentum
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin Inhibitor V, subunit A
Length: 79 amino acids
Theoretical weight: 9.02 KDa
Source organism: Fagopyrum esculentum
Expression system: Escherichia coli
UniProt:
- Canonical: Q9S9F3 (Residues: 1-69; Coverage: 100%)
Structure domains: Trypsin Inhibitor V, subunit A
