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:
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Peptidase S1, PA clan, chymotrypsin-like fold
- Trypsin Inhibitor-like, cysteine rich domain
- Serine protease inhibitor-like superfamily
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan
Structure domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133213 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Activated factor Xa heavy chain
Molecule details ›
Chain: H
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
Factor X light chain
Molecule details ›
Chain: L
Length: 54 amino acids
Theoretical weight: 5.85 KDa
Source organism: Homo sapiens
UniProt:
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
Length: 54 amino acids
Theoretical weight: 5.85 KDa
Source organism: Homo sapiens
UniProt:
- Canonical: P00742 (Residues: 125-178; Coverage: 12%)
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
TIL domain-containing protein
