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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EYF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EYF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNK:(2R,4S)-2-{(R)-CARBOXY[(PHENYLACETYL)AMINO]METHYL}-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>PNK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNK:(2R,4S)-2-{(R)-CARBOXY[(PHENYLACETYL)AMINO]METHYL}-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>PNK</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyf OCA], [https://pdbe.org/4eyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eyf RCSB], [https://www.ebi.ac.uk/pdbsum/4eyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyf ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyf OCA], [https://pdbe.org/4eyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eyf RCSB], [https://www.ebi.ac.uk/pdbsum/4eyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://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.
[https://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 ==
The beta-lactam antibiotics have long been a cornerstone for the treatment of bacterial disease. Recently, a readily transferable antibiotic resistance factor called the New Delhi metallo-beta-lactamase-1 (NDM-1) has been found to confer enteric bacteria resistance to nearly all beta-lactams, including the heralded carbapenems, posing a serious threat to human health. The crystal structure of NDM-1 bound to meropenem shows for the first time the molecular details of how carbapenem antibiotics are recognized by dizinc-containing metallo-beta-lactamases. Additionally, product complex structures of hydrolyzed benzylpenicillin-, methicillin-, and oxacillin-bound NDM-1 have been solved to 1.8, 1.2, and 1.2 A, respectively, and represent the highest-resolution structural data for any metallo-beta-lactamase reported to date. Finally, we present the crystal structure of NDM-1 bound to the potent competitive inhibitor l-captopril, which reveals a unique binding mechanism. An analysis of the NDM-1 active site in these structures reveals key features important for the informed design of novel inhibitors of NDM-1 and other metallo-beta-lactamases.
New Delhi Metallo-beta-Lactamase: Structural Insights into beta-Lactam Recognition and Inhibition.,King DT, Worrall LJ, Gruninger R, Strynadka NC J Am Chem Soc. 2012 Jul 18;134(28):11362-5. Epub 2012 Jul 5. PMID:22713171<ref>PMID:22713171</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4eyf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

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