5k1f: Difference between revisions
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<StructureSection load='5k1f' size='340' side='right'caption='[[5k1f]], [[Resolution|resolution]] 1.94Å' scene=''> | <StructureSection load='5k1f' size='340' side='right'caption='[[5k1f]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5k1f]] is a 1 chain structure with sequence from [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</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=' | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella aerogenes]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: An | [[Category: An YJ]] | ||
[[Category: Cha | [[Category: Cha SS]] | ||
[[Category: Na | [[Category: Na JH]] | ||
Latest revision as of 22:17, 20 September 2023
Crystal structure of a class C beta lactamase/compound2 complexCrystal structure of a class C beta lactamase/compound2 complex
Structural highlights
FunctionQ99QC1_KLEAE This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.[ARBA:ARBA00003808] Publication Abstract from PubMedNucleotides 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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