5A28

Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,3,4-oxadiazole inhibitor.

Summary for 5A28

• Entry DOI: 10.2210/pdb5a28/pdb
• Related: 5A27
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, TETRADECANOYL-COA, 4-(4-chloro-2-{5-[(trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl}phenoxy)piperidine, ... (5 entities in total)
• Functional Keywords: transferase, myristoylation, inhibitor, drug design
• Biological source: LEISHMANIA MAJOR
• Total number of polymer chains: 1
• Total formula weight: 48914.21

Authors

Rackham, M.D.,Yu, Z.,Brannigan, J.A.,Heal, W.P.,Paape, D.,Barker, K.V.,Wilkinson, A.J.,Smith, D.F.,Tate, E.W.,Leatherbarrow, R.J. (deposition date: 2015-05-15, release date: 2016-03-23, Last modification date: 2024-05-08)

Primary citation

Rackham, M.D.,Yu, Z.,Brannigan, J.A.,Heal, W.P.,Paape, D.,Barker, K.V.,Wilkinson, A.J.,Smith, D.F.,Leatherbarrow, R.J.,Tate, E.W.
Discovery of High Affinity Inhibitors of Leishmania Donovani N-Myristoyltransferase.
Medchemcomm, 6:1761-, 2015

PubMed Abstract: -Myristoyltransferase (NMT) is a potential drug target in parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.

PubMed: 26962429
DOI: 10.1039/C5MD00241A

Experimental method

X-RAY DIFFRACTION (1.48 Å)