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Eric C. Niederhoffer, Ph.D.

Associate Professor of Biochemistry and Molecular Biology

Southern Illinois University School of Medicine
600 Agriculture Drive, Carbondale, IL 62901-6503
Rm 112 Lindegren, 618-453-6467
eniederhoffer@siumed.edu
Copyright 2000- , E.C. Niederhoffer.
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Enolase (1one) from Saccharomyces cerevisiae

Larsen, T. M., J. E. Wedekind, L. Rayment, and G. H. Reed. 1996. 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 Å resolution. Biochemistry 35:4349-4358.

Enolase (1one)

Active Site Views

  • Push the button  to observe the following residues located near the 2-phospho-D-glycerate and Mg2+:
Ala38, Arg374, Asp246, Asp320, Glu168, Glu211, Glu295, His159, His373, Lys345, Lys396, Ser39, Ser375, and three water molecules
  • Push the button  to observe the following residues located near the phosphoenolpyruvate and Mg2+:
Ala38, Arg374, Asp 246, Asp320, Glu168, Glu211, Glu295, His159, His373, Lys345, Lys396, Ser39, Ser375, and three water molecules

Push button  for Original View

 

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For more information or comments about this page contact:
eniederhoffer@siumed.edu