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):
Activated factor Xa heavy chain
Molecule details ›
Chain: D
Length: 255 amino acids
Theoretical weight: 28.65 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 255 amino acids
Theoretical weight: 28.65 KDa
Source organism: Homo sapiens
UniProt:
- Canonical:
P00742 (Residues: 235-480, 481-488; Coverage: 56%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Factor X light chain
Molecule details ›
Chain: F
Length: 96 amino acids
Theoretical weight: 10.53 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains:
Structure domains: Laminin
Length: 96 amino acids
Theoretical weight: 10.53 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00742 (Residues: 84-179; Coverage: 21%)
Sequence domains:
Structure domains: Laminin
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P3121
