1IDE
ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)
Summary for 1IDE
| Entry DOI | 10.2210/pdb1ide/pdb |
| Descriptor | ISOCITRATE DEHYDROGENASE, MAGNESIUM ION, ISOCITRIC ACID, ... (5 entities in total) |
| Functional Keywords | oxidoreductase (nad(a)-choh(d)) |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 46753.40 |
| Authors | Bolduc, J.M.,Dyer, D.H.,Scott, W.G.,Singer, P.,Sweet, R.M.,Koshland Junior, D.E.,Stoddard, B.L. (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 Jr., 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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