4E5D
2.2A resolution structure of a firefly luciferase-benzothiazole inhibitor complex
Summary for 4E5D
| Entry DOI | 10.2210/pdb4e5d/pdb |
| Descriptor | Luciferin 4-monooxygenase, 2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole (3 entities in total) |
| Functional Keywords | oxidoreductase, monooxygenase, photoprotein, luminescence, profiling, pubchem, luciferase, quantitative high-throughput screening, qhts, firefly luciferase, reporter-gene assays, adenylate forming enzymes, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Photinus pyralis (North American firefly) |
| Cellular location | Peroxisome : P08659 |
| Total number of polymer chains | 1 |
| Total formula weight | 61078.25 |
| Authors | Lovell, S.,Battaile, K.P.,Throne, N.,Shen, M.,Auld, D.S.,Inglese, J. (deposition date: 2012-03-14, release date: 2012-09-05, Last modification date: 2023-09-13) |
| Primary citation | Thorne, N.,Shen, M.,Lea, W.A.,Simeonov, A.,Lovell, S.,Auld, D.S.,Inglese, J. Firefly luciferase in chemical biology: a compendium of inhibitors, mechanistic evaluation of chemotypes, and suggested use as a reporter. Chem.Biol., 19:1060-1072, 2012 Cited by PubMed Abstract: Firefly luciferase (FLuc) is frequently used as a reporter in high-throughput screening assays, owing to the exceptional sensitivity, dynamic range, and rapid measurement that bioluminescence affords. However, interaction of small molecules with FLuc has, to some extent, confounded its use in chemical biology and drug discovery. To identify and characterize chemotypes interacting with FLuc, we determined potency values for 360,864 compounds found in the NIH Molecular Libraries Small Molecule Repository, available in PubChem. FLuc inhibitory activity was observed for 12% of this library with discernible SAR. Characterization of 151 inhibitors demonstrated a variety of inhibition modes, including FLuc-catalyzed formation of multisubstrate adduct enzyme inhibitor complexes. As in some cell-based FLuc reporter assays, compounds acting as FLuc inhibitors yield paradoxical luminescence increases, thus data on compounds acquired from FLuc-dependent assays require careful analysis as described here. PubMed: 22921073DOI: 10.1016/j.chembiol.2012.07.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.201 Å) |
Structure validation
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