› 1p0s

X-ray diffraction
2.8Å resolution

Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R

Released:
DOI: 10.2210/pdb1p0s/pdb
PDB entry 1p0s coloured by chain, front view.
PDB entry 1p0s coloured by chain, side view.
PDB entry 1p0s coloured by chain, top view.
Source organisms:
Primary publication:
The extended interactions and Gla domain of blood coagulation factor Xa.
Wang SX, Hur E, Sousa CA, Brinen L, Slivka EJ, Fletterick RJ
Biochemistry 42 7959-66 (2003)
PMID: 12834348

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 hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133219 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Factor X light chain Chain: L
Molecule details ›
Chain: L
Length: 138 amino acids
Theoretical weight: 16.07 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 41-178; Coverage: 30%)
Gene name: F10
Sequence domains:
Structure domains:
Activated factor Xa heavy chain Chain: H
Molecule details ›
Chain: H
Length: 254 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00742 (Residues: 235-488; Coverage: 56%)
Gene name: F10
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ecotin Chain: E
Molecule details ›
Chain: E
Length: 142 amino acids
Theoretical weight: 16.15 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P23827 (Residues: 21-162; Coverage: 100%)
Gene names: JW2197, b2209, eco, eti
Sequence domains: Ecotin
Structure domains: Ecotin

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand NA 1 x NA
1 modified residue:
Ligand CGU 11 x CGU

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: I222
Unit cell:
a: 66.839Å b: 108.05Å c: 186.305Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.234
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The blood coagulation cascade.
Schenone et al. (2004)
1 more

4 mentions without citation

Understanding selectivity of hard and soft metal cations within biological systems using the subvalence concept. I. Application to blood coagulation: direct cation-protein electronic effects vs. indirect interactions through water networks.
de Courcy et al. (2010)
3 more