View source for 6lip


==Crystal structure of NDM-1 in complex with D-captopril derivative wss0218==
<StructureSection load='6lip' size='340' side='right'caption='[[6lip]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LIP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LIP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EEL:(2R)-1-[3-sulfanyl-2-(sulfanylmethyl)propanoyl]pyrrolidine-2-carboxylic+acid'>EEL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaNDM-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lip OCA], [http://pdbe.org/6lip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lip RCSB], [http://www.ebi.ac.uk/pdbsum/6lip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lip ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/BLAN1_KLEPN BLAN1_KLEPN]] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-lactam antibiotics have long been the mainstay for the treatment of bacterial infections. New Delhi metallo-beta-lactamase 1 (NDM-1) is able to hydrolyze nearly all beta-lactam antibiotics and even clinically used serine-beta-lactamase inhibitors. The wide and rapid spreading of NDM-1 gene among pathogenic bacteria has attracted extensive attention, therefore high potency NDM-1 inhibitors are urgently needed. Here we report a series of structure-guided design of D-captopril derivatives that can inhibit the activity of NDM-1 in vitro and at cellular levels. Structural comparison indicates the mechanisms of inhibition enhancement and provides insights for further inhibitor optimization.

Structure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors.,Ma G, Wang S, Wu K, Zhang W, Ahmad A, Hao Q, Lei X, Zhang H Bioorg Med Chem. 2020 Dec 3;29:115902. doi: 10.1016/j.bmc.2020.115902. PMID:33302045<ref>PMID:33302045</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lip" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Ma, G]]
[[Category: Zhang, H]]
[[Category: Antibiotic]]
[[Category: Antibiotic resistent]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Metallo-beta-lactamase]]
[[Category: Ndm-1]]
[[Category: Thio compound]]