5N4S

VIM-2 metallo-beta-lactamase in complex with ((S)-3-mercapto-2-methylpropanoyl)-D-tryptophan (Compound 3)

5N4S の概要

• エントリーDOI: 10.2210/pdb5n4s/pdb
• 分子名称: Beta-lactamase VIM-2, ZINC ION, (2~{R})-3-(1~{H}-indol-3-yl)-2-[[(2~{S})-2-methyl-3-sulfanyl-propanoyl]amino]propanoic acid, ... (5 entities in total)
• 機能のキーワード: metallo-beta-lactamase, inhibitor, complex, antibiotic resistance, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50666.32

構造登録者

Li, G.-B.,Brem, J.,McDonough, M.A.,Schofield, C.J. (登録日: 2017-02-11, 公開日: 2017-05-17, 最終更新日: 2024-01-17)

主引用文献

Li, G.B.,Brem, J.,Lesniak, R.,Abboud, M.I.,Lohans, C.T.,Clifton, I.J.,Yang, S.Y.,Jimenez-Castellanos, J.C.,Avison, M.B.,Spencer, J.,McDonough, M.A.,Schofield, C.J.
Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.
Chem. Commun. (Camb.), 53:5806-5809, 2017

PubMed Abstract: Crystallographic analyses of the VIM-5 metallo-β-lactamase (MBL) with isoquinoline inhibitors reveal non zinc ion binding modes. Comparison with other MBL-inhibitor structures directed addition of a zinc-binding thiol enabling identification of potent B1 MBL inhibitors. The inhibitors potentiate meropenem activity against clinical isolates harboring MBLs.

PubMed: 28470248
DOI: 10.1039/c7cc02394d

実験手法

X-RAY DIFFRACTION (1.2 Å)