› 3oz7

X-ray diffraction
2.7Å resolution

Crystal Structure of 3-Phosphopglycerate Kinase of Plasmodium falciparum

Released:
DOI: 10.2210/pdb3oz7/pdb
PDB entry 3oz7 coloured by chain, front view.
PDB entry 3oz7 coloured by chain, side view.
PDB entry 3oz7 coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Crystal structure of Plasmodium falciparum phosphoglycerate kinase: evidence for anion binding in the basic patch.
Smith CD, Chattopadhyay D, Pal B
Biochem Biophys Res Commun 412 203-6 (2011)
PMID: 21798238

Function and Biology Details

Reaction catalysed: 
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 417 amino acids
Theoretical weight: 45.64 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: P27362 (Residues: 2-415; Coverage: 100%)
Gene names: PFI1105w, PGK
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6122
Unit cell:
a: 131.386Å b: 131.386Å c: 262.617Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.231 0.274
Expression system: Escherichia coli

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Citations

4 review citations

Exploiting unique structural and functional properties of malarial glycolytic enzymes for antimalarial drug development.
Alam et al. (2014)
3 more

2 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)
1 more