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1IDD

ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME

Summary for 1IDD
Entry DOI10.2210/pdb1idd/pdb
DescriptorISOCITRATE DEHYDROGENASE (1 entity in total)
Functional Keywordsoxidoreductase (nad(a)-choh(d))
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight45793.56
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 citationBolduc, 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: 7761851
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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