› 1ygc

X-ray diffraction
2Å resolution

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:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-140351 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Factor VII heavy chain Chain: H
Molecule details ›
Chain: H
Length: 254 amino acids
Theoretical weight: 28.1 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P08709 (Residues: 213-466; Coverage: 57%)
Gene name: F7
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Factor VII light chain Chain: L
Molecule details ›
Chain: L
Length: 63 amino acids
Theoretical weight: 6.87 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P08709 (Residues: 150-212; Coverage: 14%)
Gene name: F7
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand SO4 7 x SO4
Ligand 905 1 x 905
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P41212
Unit cell:
a: 95.22Å b: 95.22Å c: 116.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.205
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis.
Mackman et al. (2007)
4 more

9 mentions without citation

Variability in docking success rates due to dataset preparation.
Corbeil et al. (2012)
8 more