5A27

Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.

5A27 の概要

• エントリーDOI: 10.2210/pdb5a27/pdb
• 関連するPDBエントリー: 5A28
• 分子名称: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, TETRADECANOYL-COA, 5-chloranyl-N-[2-(3-methoxyphenyl)ethanimidoyl]-2-piperidin-4-yloxy-benzamide, ... (5 entities in total)
• 機能のキーワード: transferase, myristoylation, drug design
• 由来する生物種: LEISHMANIA MAJOR
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48914.21

構造登録者

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. (登録日: 2015-05-15, 公開日: 2016-03-23, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.37 Å)