4A22
Structure of Mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase bound to N-(4-hydroxybutyl)- glycolohydroxamic acid bis- phosphate
Summary for 4A22
Entry DOI | 10.2210/pdb4a22/pdb |
Related | 4A21 |
Descriptor | FRUCTOSE-BISPHOSPHATE ALDOLASE, 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate, SODIUM ION, ... (6 entities in total) |
Functional Keywords | lyase, lyase-inhibitor complex |
Biological source | MYCOBACTERIUM TUBERCULOSIS |
Total number of polymer chains | 4 |
Total formula weight | 148025.04 |
Authors | Coincon, M.,De la Paz Santangelo, M.,Gest, P.M.,Guerin, M.E.,Pham, H.,Ryan, G.,Puckett, S.E.,Spencer, J.S.,Gonzalez-Juarrero, M.,Daher, R.,Lenaerts, A.J.,Schnappinger, D.,Therisod, M.,Ehrt, S.,Jackson, M.,Sygusch, J. (deposition date: 2011-09-21, release date: 2011-10-12, Last modification date: 2024-05-08) |
Primary citation | de la Paz Santangelo, M.,Gest, P.M.,Guerin, M.E.,Coincon, M.,Pham, H.,Ryan, G.,Puckett, S.E.,Spencer, J.S.,Gonzalez-Juarrero, M.,Daher, R.,Lenaerts, A.J.,Schnappinger, D.,Therisod, M.,Ehrt, S.,Sygusch, J.,Jackson, M. Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli. J. Biol. Chem., 286:40219-40231, 2011 Cited by PubMed: 21949126DOI: 10.1074/jbc.M111.259440 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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