4BBH

Plasmodium vivax N-myristoyltransferase with a bound benzothiophene inhibitor

Summary for 4BBH

• Entry DOI: 10.2210/pdb4bbh/pdb
• Related: 4A95 4B10 4B11 4B12 4B13 4B14
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, DIMETHYL SULFOXIDE, 2-oxopentadecyl-CoA, ... (8 entities in total)
• Functional Keywords: transferase, myristoylation, malaria, inhibitor
• Biological source: PLASMODIUM VIVAX
• Total number of polymer chains: 3
• Total formula weight: 139517.15

Authors

Rackham, M.D.,Brannigan, J.A.,Moss, D.K.,Yu, Z.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J. (deposition date: 2012-09-23, release date: 2012-12-05, Last modification date: 2024-05-08)

Primary citation

Rackham, M.D.,Brannigan, J.A.,Moss, D.K.,Yu, Z.,Wilkinson, A.J.,Holder, A.A.,Tate, E.W.,Leatherbarrow, R.J.
Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium Falciparum and Plasmodium Vivax N-Myristoyltransferase.
J.Med.Chem., 56:371-, 2013

PubMed Abstract: N-Myristoyltransferase (NMT) is an attractive antiprotozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE), and display antiparasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring.

PubMed: 23170970
DOI: 10.1021/JM301474T

Experimental method

X-RAY DIFFRACTION (1.63 Å)