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PDBe Entry: 1ebh 
OCTAHEDRAL COORDINATION AT THE HIGH AFFINITY METAL SITE IN ENOLASE; CRYSTALLOGRAPHIC ANALYSIS OF THE MG++-ENZYME FROM YEAST AT 1.9 ANGSTROMS RESOLUTION
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CARBON-OXYGEN LYASE
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X-RAY DIFFRACTION
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Resolution: 1.9 Å, R-factor: 19.0%, Spacegroup: P 1 21 1
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27/04/1995, deposition: 01/11/1994, last revision: 24/02/2009
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Wedekind, J.E.; Reed, G.H.; Rayment, I.
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Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII--enzyme complex from yeast at 1.9 A resolution.
BIOCHEMISTRY vol:34, pag:4325-4330 (1995) [PubMed ID 7703246 ]
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CARBON-OXYGEN LYASE
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4.2.1.11 ExPASy BRENDA (A B)
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Saccharomyces cerevisiae(baker's yeast) 4932(A B)
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Enolase 1 (EC 4.2.1.11) (2-phosphoglycerate dehydratase 1) (2-phospho-D-glycerate hydro-lyase 1) P00924 (A B)
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A, B
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| A, B |
ENOLASE |
Protein |
P00924 (ENO1_YEAST)
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436 |
100% |
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| A, B |
CHLORIDE ION |
CL
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| A, B |
MAGNESIUM ION |
MG
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