5g13: Difference between revisions
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<StructureSection load='5g13' size='340' side='right'caption='[[5g13]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='5g13' size='340' side='right'caption='[[5g13]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5g13]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5g13]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G13 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]] 1.99Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g13 OCA], [https://pdbe.org/5g13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g13 RCSB], [https://www.ebi.ac.uk/pdbsum/5g13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g13 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HDAH_PSEAE HDAH_PSEAE] Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines.<ref>PMID:26956223</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa PAO1]] | ||
[[Category: Kraemer | [[Category: Kraemer A]] | ||
[[Category: Meyer-Almes | [[Category: Meyer-Almes FJ]] | ||
[[Category: Yildiz | [[Category: Yildiz O]] | ||