› 1oep

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192421 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
phosphopyruvate hydratase Chain: A
Molecule details ›
Chain: A
Length: 432 amino acids
Theoretical weight: 46.88 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NDH8 (Residues: 1-429; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand SO4 1 x SO4
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: C2221
Unit cell:
a: 74.018Å b: 110.536Å c: 109.098Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Glycobiology of the Leishmania parasite and emerging targets for antileishmanial drug discovery.
Chandra et al. (2010)
24 other articles

6 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 more