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:
- not assigned
Sequence domains:
- 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
- Serine proteases, trypsin family, serine active site
2 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Coagulation factor Xa complex (preferred)
PDBe Complex ID:
PDB-CPX-133209 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Factor X light chain
Molecule details ›
Chain: L
Length: 95 amino acids
Theoretical weight: 10.39 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains: Laminin
Length: 95 amino acids
Theoretical weight: 10.39 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00742 (Residues: 85-179; Coverage: 21%)
Sequence domains:
Structure domains: Laminin
Activated factor Xa heavy chain
Molecule details ›
Chain: C
Length: 235 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 235 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00742 (Residues: 235-469; Coverage: 51%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
