6jka

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<StructureSection load='6jka' size='340' side='right'caption='[[6jka]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='6jka' size='340' side='right'caption='[[6jka]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jka]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JKA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jka]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JKA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BQU:3-[2-azanyl-5-[2-(phenoxymethyl)-1,3-thiazol-4-yl]phenyl]propanoic+acid'>BQU</scene>, <scene name='pdbligand=BS0:6-[2-(phenoxymethyl)-1,3-thiazol-4-yl]-3,4-dihydro-1H-quinolin-2-one'>BS0</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=BQU:3-[2-azanyl-5-[2-(phenoxymethyl)-1,3-thiazol-4-yl]phenyl]propanoic+acid'>BQU</scene>, <scene name='pdbligand=BS0:6-[2-(phenoxymethyl)-1,3-thiazol-4-yl]-3,4-dihydro-1H-quinolin-2-one'>BS0</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jka OCA], [http://pdbe.org/6jka PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jka RCSB], [http://www.ebi.ac.uk/pdbsum/6jka PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jka ProSAT]</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=6jka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jka OCA], [https://pdbe.org/6jka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jka RCSB], [https://www.ebi.ac.uk/pdbsum/6jka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jka ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BLAB_SERMA BLAB_SERMA]] Confers resistance to imipenem and broad-spectrum beta-lactams. Also hydrolyzes carbapenems.
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[[https://www.uniprot.org/uniprot/BLAB_SERMA BLAB_SERMA]] Confers resistance to imipenem and broad-spectrum beta-lactams. Also hydrolyzes carbapenems.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metallo-beta-lactamases (MBLs) are significant threats to humans because they deteriorate many kinds of beta-lactam antibiotics and are key enzymes responsible for multi-drug resistance of bacterial pathogens. As a result of in vitro screening, two compounds were identified as potent inhibitors of two kinds of MBLs: imipenemase (IMP-1) and New Delhi metallo-beta-lactamase (NDM-1). The binding structure of one of the identified compounds was clarified by an X-ray crystal analysis in complex with IMP-1, in which two possible binding poses were observed. Molecular dynamics (MD) simulations were performed by building two calculation models from the respective binding poses. The compound was stably bound to the catalytic site during the simulation in one pose. The binding model between NDM-1 and the compound was constructed for MD simulation. Calculation results for NDM-1 were similar to those of IMP-1. The simulation suggested that the binding of the identified inhibitory compound was also durable in the catalytic site of NDM-1. The compound will be a sound basis for the development of the inhibitors for MBLs.
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Identification of the Inhibitory Compounds for Metallo-beta-lactamases and Structural Analysis of the Binding Modes.,Kamo T, Kuroda K, Kondo S, Hayashi U, Fudo S, Yoneda T, Takaya A, Nukaga M, Hoshino T Chem Pharm Bull (Tokyo). 2021;69(12):1179-1183. doi: 10.1248/cpb.c21-00611. PMID:34853284<ref>PMID:34853284</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 6jka" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 16:51, 15 December 2021

Crystal structure of metallo-beta-lactamse, IMP-1, in complex with a thiazole-bearing inhibitor

PDB ID 6jka

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