› 3kkk

X-ray diffraction
2.08Å resolution

Y92C catalytic residue mutant of Phosphoglycerate Mutase from Plasmodium falciparum

Released:
DOI: 10.2210/pdb3kkk/pdb
PDB entry 3kkk coloured by chain, front view.
PDB entry 3kkk coloured by chain, side view.
PDB entry 3kkk coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Entry authors: Larson ET, Merritt EA, Medical Structural Genomics of Pathogenic Protozoa, Medical Structural Genomics of Pathogenic Protozoa (MSGPP)

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 258 amino acids
Theoretical weight: 29.79 KDa
Source organism: Plasmodium falciparum 3D7
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 71.062Å b: 76.12Å c: 101.68Å
α: 90° β: 99.68° γ: 90°
R-values:
R R work R free
0.198 0.196 0.236
Expression system: Escherichia coli

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