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2EGH

Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with a magnesium ion, NADPH and fosmidomycin

Summary for 2EGH
Entry DOI10.2210/pdb2egh/pdb
Descriptor1-deoxy-D-xylulose 5-phosphate reductoisomerase, MAGNESIUM ION, 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID, ... (5 entities in total)
Functional Keywordsprotein-inhibitor complex, oxidoreductase
Biological sourceEscherichia coli str. K12 substr.
Total number of polymer chains2
Total formula weight94253.43
Authors
Yajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Seto, H. (deposition date: 2007-03-01, release date: 2007-06-19, Last modification date: 2023-10-25)
Primary citationYajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Ohsawa, K.,Seto, H.
Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in a quaternary complex with a magnesium ion, NADPH and the antimalarial drug fosmidomycin
Acta Crystallogr.,Sect.F, 63:466-470, 2007
Cited by
PubMed Abstract: The crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) from Escherichia coli complexed with Mg(2+), NADPH and fosmidomycin was solved at 2.2 A resolution. DXR is the key enzyme in the 2-C-methyl-D-erythritol 4-phosphate pathway and is an effective target of antimalarial drugs such as fosmidomycin. In the crystal structure, electron density for the flexible loop covering the active site was clearly observed, indicating the well ordered conformation of DXR upon substrate binding. On the other hand, no electron density was observed for the nicotinamide-ribose portion of NADPH and the position of Asp149 anchoring Mg(2+) was shifted by NADPH in the active site.
PubMed: 17554164
DOI: 10.1107/S1744309107024475
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2025-08-06公开中

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