› 1pgj

X-ray diffraction
2.82Å resolution

X-RAY STRUCTURE OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM THE PROTOZOAN PARASITE T. BRUCEI

Released:
DOI: 10.2210/pdb1pgj/pdb
PDB entry 1pgj coloured by chain, front view.
PDB entry 1pgj coloured by chain, side view.
PDB entry 1pgj coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
A 2.8 A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues.
Phillips C, Dohnalek J, Gover S, Barrett MP, Adams MJ
J Mol Biol 282 667-81 (1998)
PMID: 9737929

Function and Biology Details

Reaction catalysed: 
6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH
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-151903 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphogluconate dehydrogenase, decarboxylating Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 52.09 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31072 (Residues: 2-479; Coverage: 100%)
Gene name: GND
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3121
Unit cell:
a: 135.13Å b: 135.13Å c: 116.74Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The return of metabolism: biochemistry and physiology of the pentose phosphate pathway.
Stincone et al. (2015)
1 more

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