5NAI

mono-Zinc VIM-5 metallo-beta-lactamase in complex with (1-chloro-4-hydroxyisoquinoline-3-carbonyl)-D-tryptophan (Compound 1)

Summary for 5NAI

• Entry DOI: 10.2210/pdb5nai/pdb
• Descriptor: Class B metallo-beta-lactamase, ZINC ION, (2~{R})-2-[(1-chloranyl-4-oxidanyl-isoquinolin-3-yl)carbonylamino]-3-(1~{H}-indol-3-yl)propanoic acid, ... (6 entities in total)
• Functional Keywords: metallo-beta-lactamase, inhibitor, complex, antibiotic resistance, hydrolase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 28836.63

Authors

Li, G.-B.,Brem, J.,McDonough, M.A.,Schofield, C.J. (deposition date: 2017-02-28, release date: 2017-05-17, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.15 Å)