› 2h9e

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-524064 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Activated factor Xa heavy chain Chain: H
Molecule details ›
Chain: H
Length: 233 amino acids
Theoretical weight: 26.35 KDa
Source organism: Homo sapiens
Factor X light chain Chain: L
Molecule details ›
Chain: L
Length: 149 amino acids
Theoretical weight: 16.37 KDa
Source organism: Homo sapiens
TIL domain-containing protein Chain: C
Molecule details ›
Chain: C
Length: 84 amino acids
Theoretical weight: 9.66 KDa
Source organism: Ancylostoma caninum
Expression system: Escherichia coli
selectide inhibitor DTY-ILE-ARG-LEU-LPD peptide Chain: S
Molecule details ›
Chain: S
Length: 5 amino acids
Theoretical weight: 661 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand PO4 6 x PO4
Ligand ACT 3 x ACT
Ligand NA 1 x NA
2 modified residues:
Ligand DTY 1 x DTY
Ligand LPD 1 x LPD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 48.945Å b: 86.41Å c: 145.892Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.22 0.268
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Exosites in the substrate specificity of blood coagulation reactions.
Bock et al. (2007)
3 more

4 mentions without citation

Dynamical view of membrane binding and complex formation of human factor VIIa and tissue factor.
Ohkubo et al. (2010)
3 more