Function and Biology Details
Reaction catalysed:
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- EGF-like domain
- Gamma-carboxyglutamic acid-rich (GLA) domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
5 more domains
Structure domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Activated factor Xa heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-133208 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Factor X light chain
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 15.21 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Length: 134 amino acids
Theoretical weight: 15.21 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00742 (Residues: 46-179; Coverage: 29%)
Sequence domains:
- Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain
- EGF-like domain
- Coagulation Factor Xa inhibitory site
Activated factor Xa heavy chain
Molecule details ›
Chain: B
Length: 254 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 254 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00742 (Residues: 235-488; Coverage: 56%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
