› 3pgm

X-ray diffraction
2.8Å resolution

THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION

Released:
DOI: 10.2210/pdb3pgm/pdb
PDB entry 3pgm coloured by chain, front view.
PDB entry 3pgm coloured by chain, side view.
PDB entry 3pgm coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure and activity of phosphoglycerate mutase.
Winn SI, Watson HC, Harkins RN, Fothergill LA
Philos Trans R Soc Lond B Biol Sci 293 121-30 (1981)
PMID: 6115412

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
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 27.17 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P00950 (Residues: 2-247; Coverage: 99%)
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 SO4 4 x SO4
Ligand 3PG 2 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 96.4Å b: 85.9Å c: 81.9Å
α: 90° β: 120.6° γ: 90°
Expression system: Not provided

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Citations

5 review citations

Enzyme catalysis: not different, just better.
Knowles JR. (1991)
4 more

7 mentions without citation

Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins.
de Souza et al. (1998)
6 more