5n4s

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

Structural highlights

5n4s is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9K2N0_PSEAI

Publication Abstract from PubMed

Crystallographic analyses of the VIM-5 metallo-beta-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.

Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.,Li GB, Brem J, Lesniak R, Abboud MI, Lohans CT, Clifton IJ, Yang SY, Jimenez-Castellanos JC, Avison MB, Spencer J, McDonough MA, Schofield CJ Chem Commun (Camb). 2017 May 4. doi: 10.1039/c7cc02394d. PMID:28470248[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Li GB, Brem J, Lesniak R, Abboud MI, Lohans CT, Clifton IJ, Yang SY, Jimenez-Castellanos JC, Avison MB, Spencer J, McDonough MA, Schofield CJ. Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition. Chem Commun (Camb). 2017 May 4. doi: 10.1039/c7cc02394d. PMID:28470248 doi:http://dx.doi.org/10.1039/c7cc02394d

5n4s, resolution 1.20Å

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OCA