› 2p3f

X-ray diffraction
3.1Å resolution

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:
Sequence domains:
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 Chain: H
Molecule details ›
Chain: H
Length: 235 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 235-469; Coverage: 51%)
Gene name: F10
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Factor X light chain Chain: L
Molecule details ›
Chain: L
Length: 54 amino acids
Theoretical weight: 5.85 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 125-178; Coverage: 12%)
Gene name: F10
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
TIL domain-containing protein Chain: N
Molecule details ›
Chain: N
Length: 78 amino acids
Theoretical weight: 8.91 KDa
Source organism: Ancylostoma caninum
UniProt:
  • Canonical: Q16940 (Residues: 23-100; Coverage: 96%)
Sequence domains: Trypsin Inhibitor like cysteine rich domain
Structure domains: Laminin

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 137.17Å b: 137.17Å c: 167.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.28

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Citations

1 review citation

Will warfarin soon be passé? New approaches to stroke prevention in atrial fibrillation.
Hammwöhner et al. (2008)
9 other articles