1IDD
ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME
Summary for 1IDD
Entry DOI | 10.2210/pdb1idd/pdb |
Descriptor | ISOCITRATE DEHYDROGENASE (1 entity in total) |
Functional Keywords | oxidoreductase (nad(a)-choh(d)) |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 45793.56 |
Authors | Lee, M.E.,Dyer, D.H.,Klein, O.D.,Bolduc, J.M.,Stoddard, B.L.,Koshland Junior, D.E. (deposition date: 1995-01-18, release date: 1996-03-08, Last modification date: 2024-02-07) |
Primary citation | Bolduc, J.M.,Dyer, D.H.,Scott, W.G.,Singer, P.,Sweet, R.M.,Koshland, D.E.,Stoddard, B.L. Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science, 268:1312-1318, 1995 Cited by PubMed Abstract: Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized. PubMed: 7761851PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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