› 1bq3

X-ray diffraction
2.7Å resolution

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE

Released:
DOI: 10.2210/pdb1bq3/pdb
PDB entry 1bq3 coloured by chain, front view.
PDB entry 1bq3 coloured by chain, side view.
PDB entry 1bq3 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.
Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA
J Mol Biol 289 691-9 (1999)
PMID: 10369755

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133712 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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:
Ligand IHP 2 x IHP
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 82.58Å b: 93.38Å c: 148.56Å
α: 90° β: 90.13° γ: 90°
R-values:
R R work R free
0.2 0.2 0.24

Quick links

Citations

5 review citations

Anticancer agents that counteract tumor glycolysis.
Granchi et al. (2012)
4 more

2 mentions without citation

From the similarity analysis of protein cavities to the functional classification of protein families using cavbase.
Kuhn et al. (2006)
1 more