1IDC
ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY
1IDC の概要
エントリーDOI | 10.2210/pdb1idc/pdb |
分子名称 | ISOCITRATE DEHYDROGENASE, MAGNESIUM ION, 2-OXALOSUCCINIC ACID (3 entities in total) |
機能のキーワード | oxidoreductase (nad(a)-choh(d)) |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 46025.99 |
構造登録者 | Bolduc, J.M.,Dyer, D.H.,Scott, W.G.,Singer, P.,Sweet, R.M.,Koshland Junior, D.E.,Stoddard, B.L. (登録日: 1995-01-18, 公開日: 1996-03-08, 最終更新日: 2024-12-25) |
主引用文献 | 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: 7761851主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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