3EKL
Structural Characterization of tetrameric Mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase - substrate binding and catalysis mechanism of a class IIa bacterial aldolase
Summary for 3EKL
Entry DOI | 10.2210/pdb3ekl/pdb |
Related | 3EKB 3ELF |
Descriptor | Fructose-bisphosphate aldolase, 1,3-DIHYDROXYACETONEPHOSPHATE, ZINC ION, ... (5 entities in total) |
Functional Keywords | class ii fructose-1, 6-bisphosphate aldolase, zinc enzyme, mycobacterium tuberculosis, dihydroxyacetone, glyceraldehyde-3-phosphate, aldol condensation, glycolysis, lyase, metal-binding, zinc |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 37770.03 |
Authors | Pegan, S.,Rukseree, K.,Franzblau, S.G.,Mesecar, A.D. (deposition date: 2008-09-19, release date: 2009-02-10, Last modification date: 2023-08-30) |
Primary citation | Pegan, S.D.,Rukseree, K.,Franzblau, S.G.,Mesecar, A.D. Structural basis for catalysis of a tetrameric class IIa fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis J.Mol.Biol., 386:1038-1053, 2009 Cited by PubMed: 19167403DOI: 10.1016/j.jmb.2009.01.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
Download full validation report