5k1f: Difference between revisions

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-'''Unreleased structure'''
-The entry 5k1f is ON HOLD  until Paper Publication
+==Crystal structure of a class C beta lactamase/compound2 complex==
+<StructureSection load='5k1f' size='340' side='right'caption='[[5k1f]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5k1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K1F FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</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=5k1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1f OCA], [https://pdbe.org/5k1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k1f RCSB], [https://www.ebi.ac.uk/pdbsum/5k1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q99QC1_KLEAE Q99QC1_KLEAE] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.[ARBA:ARBA00003808]
+<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:
+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:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5k1f" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Klebsiella aerogenes]]
+[[Category: Large Structures]]
+[[Category: An YJ]]
+[[Category: Cha SS]]
+[[Category: Na JH]]