4UCM
CRYSTAL STRUCTURE OF LEISHMANIA MAJOR N-MYRISTOYLTRANSFERASE (NMT) WITH BOUND MYRISTOYL-COA AND A FRAGMENT
Summary for 4UCM
| Entry DOI | 10.2210/pdb4ucm/pdb |
| Related | 4UCN 4UCP |
| Descriptor | GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, TETRADECANOYL-COA, methyl-3-methyl-5-phenyl-2H-pyrazol-4-methyl amine, ... (4 entities in total) |
| Functional Keywords | nmt, myristoyltransferase, acyltransferase, transferase, drug discovery, fragment |
| Biological source | LEISHMANIA MAJOR |
| Total number of polymer chains | 1 |
| Total formula weight | 51692.41 |
| Authors | Robinson, D.A.,Wyatt, P.G. (deposition date: 2014-12-04, release date: 2015-05-13, Last modification date: 2023-12-20) |
| Primary citation | Robinson, D.A.,Wyatt, P.G. Identification and Structure Solution of Fragment Hits Against Kinetoplastid N-Myristoyltransferase Acta Crystallogr.,Sect.F, 71:586-, 2015 Cited by PubMed Abstract: Trypanosoma brucei N-myristoyltransferase (TbNMT) is an attractive therapeutic target for the treatment of human African trypanosomiasis. Pyrazole sulfonamide (DDD85646), a potent inhibitor of TbNMT, has been identified in previous studies; however, poor central nervous system exposure restricts its use to the haemolymphatic form (stage 1) of the disease. In order to identify new chemical matter, a fragment screen was carried out by ligand-observed NMR spectroscopy, identifying hits that occupy the DDD85646 binding site. Crystal structures of hits from this assay have been obtained in complex with the closely related NMT from Leishmania major, providing a structural starting point for the evolution of novel chemical matter. PubMed: 25945713DOI: 10.1107/S2053230X15003040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.32 Å) |
Structure validation
Download full validation report
