1DG5
DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND TRIMETHOPRIM
Summary for 1DG5
Entry DOI | 10.2210/pdb1dg5/pdb |
Related | 1DF7 1DG7 1DG8 |
Descriptor | DIHYDROFOLATE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TRIMETHOPRIM, ... (5 entities in total) |
Functional Keywords | dihydrofolate reductase, structure-based inhibitor design, folateanalogs, rossmann fold, nicotinamide adenine dinucleotide, trimethoprim, tuberculosis, oxidoreductase |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 18973.01 |
Authors | Li, R.,Sirawaraporn, R.,Chitnumsub, P.,Sirawaraporn, W.,Wooden, J.,Athappilly, F.,Turley, S.,Hol, W.G. (deposition date: 1999-11-23, release date: 2000-03-09, Last modification date: 2024-02-07) |
Primary citation | Li, R.,Sirawaraporn, R.,Chitnumsub, P.,Sirawaraporn, W.,Wooden, J.,Athappilly, F.,Turley, S.,Hol, W.G. Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. J.Mol.Biol., 295:307-323, 2000 Cited by PubMed: 10623528DOI: 10.1006/jmbi.1999.3328 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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