1DFI
X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD
Summary for 1DFI
| Entry DOI | 10.2210/pdb1dfi/pdb |
| Descriptor | ENOYL ACYL CARRIER PROTEIN REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | oxidoreductase, lipid biosynthesis |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 113700.62 |
| Authors | Baldock, C.,Rafferty, J.B.,Rice, D.W. (deposition date: 1997-01-16, release date: 1998-01-28, Last modification date: 2024-05-22) |
| Primary citation | Baldock, C.,Rafferty, J.B.,Sedelnikova, S.E.,Baker, P.J.,Stuitje, A.R.,Slabas, A.R.,Hawkes, T.R.,Rice, D.W. A mechanism of drug action revealed by structural studies of enoyl reductase. Science, 274:2107-2110, 1996 Cited by PubMed Abstract: Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry. PubMed: 8953047DOI: 10.1126/science.274.5295.2107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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