5k1d: Difference between revisions

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'''Unreleased structure'''


The entry 5k1d is ON HOLD
==Crystal structure of a class C beta lactamase/compound1 complex==
<StructureSection load='5k1d' size='340' side='right' caption='[[5k1d]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5k1d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K1D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k1f|5k1f]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1d OCA], [http://pdbe.org/5k1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k1d RCSB], [http://www.ebi.ac.uk/pdbsum/5k1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1d ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nucleotides were effective in inhibiting the class C beta-lactamase CMY-10. IMP was the most potent competitive inhibitor, with a Ki value of 16.2 muM. The crystal structure of CMY-10 complexed with GMP or IMP revealed that nucleotides fit into the R2 subsite of the active site with a unique vertical binding mode where the phosphate group at one terminus is deeply bound in the subsite and the base at the other terminus faces the solvent.


Authors: AN, Y.J., Na, J.H., Cha, S.S.
GMP and IMP Are Competitive Inhibitors of CMY-10, an Extended-Spectrum Class C beta-Lactamase.,Na JH, An YJ, Cha SS Antimicrob Agents Chemother. 2017 Apr 24;61(5). pii: e00098-17. doi:, 10.1128/AAC.00098-17. Print 2017 May. PMID:28242658<ref>PMID:28242658</ref>


Description: Crystal structure of a class C beta lactamase/compound1 complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Na, J.H]]
<div class="pdbe-citations 5k1d" style="background-color:#fffaf0;"></div>
[[Category: Cha, S.S]]
== References ==
[[Category: An, Y.J]]
<references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: AN, Y J]]
[[Category: Cha, S S]]
[[Category: Na, J H]]
[[Category: Class c beta-lactamase]]
[[Category: Hydrolase]]
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