5g13: Difference between revisions

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==Pseudomonas aeruginosa HDAH (H143A) unliganded.==
==Pseudomonas aeruginosa HDAH (H143A) unliganded.==
<StructureSection load='5g13' size='340' side='right' caption='[[5g13]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='5g13' size='340' side='right'caption='[[5g13]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5g13]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G13 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g0x|5g0x]], [[5g0y|5g0y]], [[5g10|5g10]], [[5g11|5g11]], [[5g12|5g12]], [[5g17|5g17]], [[5g1a|5g1a]], [[5g1b|5g1b]], [[5g1c|5g1c]]</td></tr>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g13 OCA], [http://pdbe.org/5g13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g13 RCSB], [http://www.ebi.ac.uk/pdbsum/5g13 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g13 ProSAT]</span></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=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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Kraemer, A]]
[[Category: Large Structures]]
[[Category: Meyer-Almes, F J]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Yildiz, O]]
[[Category: Kraemer A]]
[[Category: Hdac]]
[[Category: Meyer-Almes FJ]]
[[Category: Hdah]]
[[Category: Yildiz O]]
[[Category: Hdlp]]
[[Category: Hydrolase]]

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