1EVZ
CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD
1EVZ の概要
| エントリーDOI | 10.2210/pdb1evz/pdb |
| 関連するPDBエントリー | 1EVY |
| 分子名称 | GLYCEROL-3-PHOSPHATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PENTADECANE, ... (4 entities in total) |
| 機能のキーワード | dehydrogenase, rossmann fold, oxidoreductase |
| 由来する生物種 | Leishmania mexicana |
| 細胞内の位置 | Glycosome: P90551 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 40193.67 |
| 構造登録者 | Suresh, S.,Turley, S.,Opperdoes, F.R.,Michels, P.A.M.,Hol, W.G.J. (登録日: 2000-04-21, 公開日: 2001-02-22, 最終更新日: 2024-02-07) |
| 主引用文献 | Suresh, S.,Turley, S.,Opperdoes, F.R.,Michels, P.A.,Hol, W.G. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure Fold.Des., 8:541-552, 2000 Cited by PubMed Abstract: NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. Although the enzyme has been characterized and cloned from a number of sources, until now no three-dimensional structure has been determined for this enzyme. Although the utility of this enzyme as a drug target against Leishmania mexicana is yet to be established, the critical role played by GPDH in the long slender bloodstream form of the related kinetoplastid Trypanosoma brucei makes it a viable drug target against sleeping sickness. PubMed: 10801498DOI: 10.1016/S0969-2126(00)00135-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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