1ONE
YEAST ENOLASE COMPLEXED WITH AN EQUILIBRIUM MIXTURE OF 2'-PHOSPHOGLYCEATE AND PHOSPHOENOLPYRUVATE
Summary for 1ONE
Entry DOI | 10.2210/pdb1one/pdb |
Descriptor | ENOLASE, MAGNESIUM ION, PHOSPHOENOLPYRUVATE, ... (5 entities in total) |
Functional Keywords | lyase, glycolysis |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Cytoplasm: P00924 |
Total number of polymer chains | 2 |
Total formula weight | 94271.01 |
Authors | Larsen, T.M.,Wedekind, J.E.,Rayment, I.,Reed, G.H. (deposition date: 1995-12-05, release date: 1997-01-11, Last modification date: 2024-02-14) |
Primary citation | Larsen, T.M.,Wedekind, J.E.,Rayment, I.,Reed, G.H. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry, 35:4349-4358, 1996 Cited by PubMed: 8605183DOI: 10.1021/bi952859c PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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