1EBG
CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION
Summary for 1EBG
Entry DOI | 10.2210/pdb1ebg/pdb |
Descriptor | ENOLASE, MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID, ... (4 entities in total) |
Functional Keywords | carbon-oxygen lyase |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Cytoplasm: P00924 |
Total number of polymer chains | 2 |
Total formula weight | 93872.91 |
Authors | Wedekind, J.E.,Reed, G.H.,Rayment, I. (deposition date: 1994-04-27, release date: 1995-04-27, Last modification date: 2024-02-07) |
Primary citation | Wedekind, J.E.,Poyner, R.R.,Reed, G.H.,Rayment, I. Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution. Biochemistry, 33:9333-9342, 1994 Cited by PubMed: 8049235DOI: 10.1021/bi00197a038 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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