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:
- 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 domain
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Coagulation factor VIIa complex (preferred)
PDBe Complex ID:
PDB-CPX-140351 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Factor VII light chain
Molecule details ›
Chain: L
Length: 104 amino acids
Theoretical weight: 11.38 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
Sequence domains:
Structure domains: Laminin
Length: 104 amino acids
Theoretical weight: 11.38 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
- Canonical:
P08709 (Residues: 109-212; Coverage: 23%)
Sequence domains:
Structure domains: Laminin
Factor VII heavy chain
Molecule details ›
Chain: H
Length: 254 amino acids
Theoretical weight: 28.1 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 254 amino acids
Theoretical weight: 28.1 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
- Canonical: P08709 (Residues: 213-466; Coverage: 57%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
