1xq9

X-ray diffraction
2.58Å resolution

Structure of Phosphoglycerate Mutase from Plasmodium falciparum at 2.6 Resolution

Released:
Source organism: Plasmodium falciparum
Entry authors: Caruthers JM, Hol WGJ, Structural Genomics of Pathogenic Protozoa Consortium (SGPP)

Function and Biology Details

Reaction catalysed:
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-184784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 29.85 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IIG6 (Residues: 1-250; Coverage: 100%)
Gene name: PF3D7_1120100
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 121.241Å b: 71.516Å c: 74.883Å
α: 90° β: 113.79° γ: 90°
R-values:
R R work R free
0.211 0.207 0.272
Expression system: Escherichia coli