5OIN
InhA (T2A mutant) complexed with N-(1-(pyrimidin-2-yl)piperidin-4-yl)acetamide
Summary for 5OIN
| Entry DOI | 10.2210/pdb5oin/pdb |
| Descriptor | Enoyl-[acyl-carrier-protein] reductase [NADH], NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ~{N}-(1-pyrimidin-2-ylpiperidin-4-yl)ethanamide, ... (4 entities in total) |
| Functional Keywords | inhibitor, complex, fragment based drug discovery, tuberculosis, oxidoreductase |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 4 |
| Total formula weight | 117413.53 |
| Authors | Convery, M.A. (deposition date: 2017-07-19, release date: 2018-02-14, Last modification date: 2024-05-08) |
| Primary citation | Prati, F.,Zuccotto, F.,Fletcher, D.,Convery, M.A.,Fernandez-Menendez, R.,Bates, R.,Encinas, L.,Zeng, J.,Chung, C.W.,De Dios Anton, P.,Mendoza-Losana, A.,Mackenzie, C.,Green, S.R.,Huggett, M.,Barros, D.,Wyatt, P.G.,Ray, P.C. Screening of a Novel Fragment Library with Functional Complexity against Mycobacterium tuberculosis InhA. ChemMedChem, 13:672-677, 2018 Cited by PubMed Abstract: Our findings reported herein provide support for the benefits of including functional group complexity (FGC) within fragments when screening against protein targets such as Mycobacterium tuberculosis InhA. We show that InhA fragment actives with FGC maintained their binding pose during elaboration. Furthermore, weak fragment hits with functional group handles also allowed for facile fragment elaboration to afford novel and potent InhA inhibitors with good ligand efficiency metrics for optimization. PubMed: 29399991DOI: 10.1002/cmdc.201700774 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.82 Å) |
Structure validation
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