2q1j

X-ray diffraction
1.9Å resolution

The discovery of glycine and related amino acid-based factor xa inhibitors

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Activated factor Xa heavy chain Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 26.45 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 235-468; Coverage: 51%)
Gene name: F10
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Factor X light chain Chain: B
Molecule details ›
Chain: B
Length: 51 amino acids
Theoretical weight: 5.46 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 128-178; Coverage: 11%)
Gene name: F10
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 56.896Å b: 72.741Å c: 78.335Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.272