5n55: Difference between revisions
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==mono-Zinc VIM-5 metallo-beta-lactamase in complex with (1-chloro-4-hydroxyisoquinoline-3-carbonyl)-L-tryptophan (Compound 2)== | |||
<StructureSection load='5n55' size='340' side='right' caption='[[5n55]], [[Resolution|resolution]] 1.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n55]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N55 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8NN:(1-CHLORO-4-HYDROXYISOQUINOLINE-3-CARBONYL)-L-TRYPTOPHAN'>8NN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=00C:3-SULFO-D-ALANINE'>00C</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n55 OCA], [http://pdbe.org/5n55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n55 RCSB], [http://www.ebi.ac.uk/pdbsum/5n55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n55 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:28470248</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5n55" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brem, J]] | [[Category: Brem, J]] | ||
[[Category: | [[Category: Li, G B]] | ||
[[Category: Schofield, C | [[Category: McDonough, M A]] | ||
[[Category: Schofield, C J]] | |||
[[Category: Antibiotic resistance]] | |||
[[Category: Complex]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inhibitor]] | |||
[[Category: Metallo-beta-lactamase]] | |||
Revision as of 15:41, 17 May 2017
mono-Zinc VIM-5 metallo-beta-lactamase in complex with (1-chloro-4-hydroxyisoquinoline-3-carbonyl)-L-tryptophan (Compound 2)
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