3UPY
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 3upy by Molmil](/molmil-images/mine/3upy) | Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway. | 分子名称: | 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID, MAGNESIUM ION, Oxidoreductase | 著者 | Calisto, B.M, Perez-Gil, J, Fita, I, Rodriguez-Concepcion, M. | 登録日 | 2011-11-18 | 公開日 | 2012-03-28 | 最終更新日 | 2023-09-13 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Crystal structure of Brucella abortus deoxyxylulose-5-phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis. J.Biol.Chem., 287, 2012
|
|
3UPL
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 3upl by Molmil](/molmil-images/mine/3upl) | Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway. | 分子名称: | GLYCEROL, MAGNESIUM ION, Oxidoreductase | 著者 | Calisto, B.M, Perez-Gil, J, Fita, I, Rodriguez-Concepcion, M. | 登録日 | 2011-11-18 | 公開日 | 2012-03-28 | 最終更新日 | 2024-03-13 | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | 主引用文献 | Crystal structure of Brucella abortus deoxyxylulose-5-phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis. J.Biol.Chem., 287, 2012
|
|
2PMP
![Download](/newweb/media/icons/dl.png) ![Visualize](/newweb/media/icons/hoh_3d.png)
![BU of 2pmp by Molmil](/molmil-images/mine/2pmp) | Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from the isoprenoid biosynthetic pathway of Arabidopsis thaliana | 分子名称: | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, CHLORIDE ION, CYTIDINE-5'-MONOPHOSPHATE, ... | 著者 | Calisto, B.M, Perez-Gil, J, Querol-Audi, J, Fita, I, Imperial, S. | 登録日 | 2007-04-23 | 公開日 | 2007-09-18 | 最終更新日 | 2023-08-30 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | Biosynthesis of isoprenoids in plants: Structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes. Protein Sci., 16, 2007
|
|