› 1fzt

Solution NMR

SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE

Released:
DOI: 10.2210/pdb1fzt/pdb
PDB entry 1fzt coloured by chain, ensemble of 21 models, front view.
PDB entry 1fzt coloured by chain, ensemble of 21 models, side view.
PDB entry 1fzt coloured by chain, ensemble of 21 models, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.
Uhrínová S, Uhrín D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN
J Mol Biol 306 275-90 (2001)
PMID: 11237600

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.8 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P36623 (Residues: 1-211; Coverage: 100%)
Gene names: SPAC26F1.06, gpm1
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
Refinement method: simulated annealing, molecular dynamics
Expression system: Saccharomyces cerevisiae

Quick links

Citations

9 citation in other articles

Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity.
Rigden et al. (2002)
8 more

3 mentions without citation

Probability-based protein secondary structure identification using combined NMR chemical-shift data.
Wang et al. (2002)
2 more