5G1Z
Plasmodium vivax N-myristoyltransferase in complex with a quinoline inhibitor (compound 1)
Summary for 5G1Z
| Entry DOI | 10.2210/pdb5g1z/pdb |
| Related | 5G20 5G21 5G22 |
| Descriptor | GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, 2-oxopentadecyl-CoA, ethyl 4-(2-cyanoethylsulfanyl)-6-methoxy-quinoline-3-carboxylate, ... (8 entities in total) |
| Functional Keywords | transferase, myristoylation, malaria, inhibitor, quinoline, drug design |
| Biological source | PLASMODIUM VIVAX (MALARIA PARASITE P. VIVAX) |
| Total number of polymer chains | 3 |
| Total formula weight | 139787.48 |
| Authors | Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W. (deposition date: 2016-04-06, release date: 2017-02-15, Last modification date: 2024-05-08) |
| Primary citation | Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. Medchemcomm, 8:191-197, 2017 Cited by PubMed Abstract: The parasite is the most widely distributed cause of recurring malaria. -Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both and -myristoyltransferase (NMT). PubMed: 28626547DOI: 10.1039/c6md00531d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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