4UFX
Plasmodium vivax N-myristoyltransferase in complex with a pyridyl inhibitor (compound 19)
Summary for 4UFX
| Entry DOI | 10.2210/pdb4ufx/pdb |
| Related | 4UFV 4UFW |
| Descriptor | GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, N-[2-(3-methoxyphenyl)ethanimidoyl]-2-piperidin-4-yloxy-pyridine-3-carboxamide, 2-oxopentadecyl-CoA, ... (8 entities in total) |
| Functional Keywords | transferase, myristoylation, malaria, inhibitor, pyridyl |
| Biological source | PLASMODIUM VIVAX (MALARIA PARASITE P. VIVAX) |
| Total number of polymer chains | 3 |
| Total formula weight | 140182.24 |
| Authors | Yu, Z.,Brannigan, J.A.,Rangachari, K.,Heal, W.P.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J. (deposition date: 2015-03-19, release date: 2016-02-03, Last modification date: 2024-05-08) |
| Primary citation | Yu, Z.,Brannigan, J.A.,Rangachari, K.,Heal, W.P.,Wilkinson, A.J.,Holder, A.A.,Leatherbarrow, R.J.,Tate, E.W. Discovery of Pyridyl-Based Inhibitors of Plasmodium Falciparum N-Myristoyltransferase Medchemcomm, 6:1767-, 2015 Cited by PubMed Abstract: -Myristoyltransferase (NMT) represents an attractive drug target in parasitic infections such as malaria due to its genetic essentiality and amenability to inhibition by drug-like small molecules. Scaffold simplification from previously reported inhibitors containing bicyclic cores identified phenyl derivative , providing a versatile platform to study the effects of substitution on the scaffold, which yielded pyridyl . This molecule exhibited improved enzyme and cellular potency, and reduced lipophilicity compared to inhibitor . Further structure-based inhibitor design led to the discovery of , the most potent inhibitor in this series, which showed single-digit nM enzyme affinity and sub-μM anti-plasmodial activity. PubMed: 26962430DOI: 10.1039/C5MD00242G PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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