3TU9
Crystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphate
Summary for 3TU9
| Entry DOI | 10.2210/pdb3tu9/pdb |
| Descriptor | Fructose-bisphosphate aldolase A, 2-O-methyl-1,6-di-O-phosphono-D-mannitol (3 entities in total) |
| Functional Keywords | beta-barrel, mammalian aldolase, mannitol-bisphosphate, trypanosomal aldolase, inhibitor docking, lyase-lyase inhibitor complex, lyase/lyase inhibitor |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm, myofibril, sarcomere, I band : P00883 |
| Total number of polymer chains | 4 |
| Total formula weight | 158479.32 |
| Authors | Arthus-Cartier, G.,Sygusch, J. (deposition date: 2011-09-16, release date: 2011-10-12, Last modification date: 2023-09-13) |
| Primary citation | Mabiala-Bassiloua, C.G.,Arthus-Cartier, G.,Hannaert, V.,Therisod, H.,Sygusch, J.,Therisod, M. Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases. ACS Med Chem Lett, 2:804-808, 2011 Cited by PubMed Abstract: Several 5-O-alkyl- and 5-C-alkyl-mannitol bis-phosphates were synthesized and comparatively assayed as inhibitors of fructose bis-phosphate aldolases (Fbas) from rabbit muscle (taken as surrogate model of the human enzyme) and from Trypanosoma brucei. A limited selectivity was found in several instances. Crystallographic studies confirm that the 5-O-methyl derivative binds competitively with substrate and the 5-O-methyl moiety penetrating deeper into a shallow hydrophobic pocket at the active site. This observation can lead to the preparation of selective competitive or irreversible inhibitors of the parasite Fba. PubMed: 24900268DOI: 10.1021/ml200129s PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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