X-ray diffraction
1.7Å resolution

Crystal structure of phosphoglycerate mutase from M. Tuberculosis


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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 265 amino acids
Theoretical weight: 29 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
  • Canonical: P9WIC9 (Residues: 1-249; Coverage: 100%)
Gene names: MTCY20G9.15, Rv0489, gpm, gpm1, gpmA, pgm
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
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 58.914Å b: 136.79Å c: 65.929Å
α: 90° β: 97.78° γ: 90°
R R work R free
0.221 not available 0.27
Expression system: Escherichia coli