Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Gamma-carboxyglutamic acid-rich (GLA) domain
- EGF-like domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- EGF-type aspartate/asparagine hydroxylation site
- EGF-like calcium-binding, conserved site
- EGF-like calcium-binding domain
5 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Coagulation factor IXa light chain (preferred)
PDBe Complex ID:
PDB-CPX-147674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coagulation factor IXa heavy chain
Molecule details ›
Chain: C
Length: 235 amino acids
Theoretical weight: 26.05 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 235 amino acids
Theoretical weight: 26.05 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
- Canonical:
P16293 (Residues: 183-409; Coverage: 56%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Coagulation factor IXa light chain
Molecule details ›
Chain: L
Length: 146 amino acids
Theoretical weight: 17 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
Sequence domains:
Length: 146 amino acids
Theoretical weight: 17 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
- Canonical: P16293 (Residues: 1-147; Coverage: 36%)
Sequence domains:
- Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain
- EGF-like domain
- Coagulation Factor Xa inhibitory site
