5pgm

X-ray diffraction
2.12Å resolution

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-133712 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 246 amino acids
Theoretical weight: 27.52 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00950 (Residues: 2-247; Coverage: 100%)
Gene names: GPM, GPM1, YKL152C, YKL607
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21
Unit cell:
a: 82.497Å b: 93.262Å c: 147.329Å
α: 90° β: 90.15° γ: 90°
R-values:
R R work R free
0.196 0.196 0.228