6N1E
Crystal structure of X. citri phosphoglucomutase in complex with 1-methyl-glucose 6-phosphate
Summary for 6N1E
Entry DOI | 10.2210/pdb6n1e/pdb |
Descriptor | Phosphomannomutase/phosphoglucomutase, MAGNESIUM ION, 1-deoxy-7-O-phosphono-alpha-D-gluco-hept-2-ulopyranose, ... (4 entities in total) |
Functional Keywords | phosphoglucomutase, carbohydrate metabolism, isomerase |
Biological source | Xanthomonas citri |
Total number of polymer chains | 1 |
Total formula weight | 51435.96 |
Authors | Beamer, L.J.,Stiers, K.M. (deposition date: 2018-11-08, release date: 2019-05-01, Last modification date: 2023-10-11) |
Primary citation | Zhu, J.S.,Stiers, K.M.,Winter, S.M.,Garcia, A.D.,Versini, A.F.,Beamer, L.J.,Jakeman, D.L. Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition. Acs Omega, 4:7029-7037, 2019 Cited by PubMed Abstract: Glucokinase phosphorylated a series of C-1 fluorinated α-d-gluco-heptuloses. These phosphorylated products were discovered to be inhibitors of α-phosphomannomutase/phosphoglucomutase (αPMM/PGM) and β-phosphoglucomutase (βPGM). Inhibition potency with both mutases inversely correlated to the degree of fluorination. Structural analysis with αPMM demonstrated the inhibitor binding to the active site, with the phosphate in the phosphate binding site and the anomeric hydroxyl directed to the catalytic site. PubMed: 31179410DOI: 10.1021/acsomega.9b00008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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