7b3s

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==OXA-10 beta-lactamase with S67Dha modification==
==OXA-10 beta-lactamase with S67Dha modification==
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<StructureSection load='7b3s' size='340' side='right'caption='[[7b3s]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='7b3s' size='340' side='right'caption='[[7b3s]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7b3s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B3S FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B3S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</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=7b3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b3s OCA], [https://pdbe.org/7b3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b3s RCSB], [https://www.ebi.ac.uk/pdbsum/7b3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b3s ProSAT]</span></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7b3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b3s OCA], [https://pdbe.org/7b3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b3s RCSB], [https://www.ebi.ac.uk/pdbsum/7b3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b3s ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
 
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[[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI]] Hydrolyzes both carbenicillin and oxacillin.
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition.
 
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Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701<ref>PMID:35486701</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7b3s" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-lactamase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brem, J]]
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[[Category: Brem J]]
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[[Category: Lang, P A]]
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[[Category: Lang PA]]
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[[Category: Schofield, C J]]
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[[Category: Schofield CJ]]
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[[Category: Antibiotic resistance]]
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[[Category: Beta lactamase]]
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[[Category: Dehydroalanine]]
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[[Category: Hydrolase]]
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[[Category: Irreversible inhibition]]
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[[Category: Tazobactam]]
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Revision as of 14:43, 31 August 2022

OXA-10 beta-lactamase with S67Dha modification

PDB ID 7b3s

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