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4wbg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of class C beta-lactamase Mox-1 covalently complexed with aztorenam== | |
| + | <StructureSection load='4wbg' size='340' side='right'caption='[[4wbg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wbg]] is a 1 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=4WBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WBG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZR:2-({[(1Z)-1-(2-AMINO-1,3-THIAZOL-4-YL)-2-OXO-2-{[(2S,3S)-1-OXO-3-(SULFOAMINO)BUTAN-2-YL]AMINO}ETHYLIDENE]AMINO}OXY)-2-METHYLPROPANOIC+ACID'>AZR</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=4wbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wbg OCA], [https://pdbe.org/4wbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wbg RCSB], [https://www.ebi.ac.uk/pdbsum/4wbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wbg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q51578_KLEPN Q51578_KLEPN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We solved the crystal structure of a class C beta-lactamase MOX-1 complexed with an inhibitor, aztreonam, at 1.9A resolution. The main-chain oxygen of Ser315 interacts with the amide nitrogen of aztreonam. Surprisingly, compared to the free MOX-1 structure, this main-chain carboxyl changes its position significantly upon binding aztreonam. This result indicates that the interaction between MOX-1 and beta-lactams can be accompanied by conformational changes of the B3 beta-strand main chain. | ||
| - | + | A Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 in Binding Aztreonam.,Oguri T, Ishii Y, Shimizu-Ibuka A Antimicrob Agents Chemother. 2015 Jun 8. pii: AAC.04428-14. PMID:26055361<ref>PMID:26055361</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4wbg" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Klebsiella pneumoniae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ishii Y]] | ||
| + | [[Category: Oguri T]] | ||
| + | [[Category: Shimizu-ibuka A]] | ||
Current revision
Crystal structure of class C beta-lactamase Mox-1 covalently complexed with aztorenam
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