3c5k

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(New page: 200px<br /><applet load="3c5k" size="350" color="white" frame="true" align="right" spinBox="true" caption="3c5k, resolution 1.55&Aring;" /> '''Crystal structure of...)
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[[Image:3c5k.jpg|left|200px]]<br /><applet load="3c5k" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3c5k, resolution 1.55&Aring;" />
 
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'''Crystal structure of human HDAC6 zinc finger domain'''<br />
 
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==About this Structure==
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==Crystal structure of human HDAC6 zinc finger domain==
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3C5K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+201'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+202'>AC2</scene> and <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+A+203'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5K OCA].
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<StructureSection load='3c5k' size='340' side='right'caption='[[3c5k]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[3c5k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C5K FirstGlance]. <br>
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[[Category: Arrowsmith, C H.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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[[Category: Bochkarev, A.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Bountra, C.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5k OCA], [https://pdbe.org/3c5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c5k RCSB], [https://www.ebi.ac.uk/pdbsum/3c5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5k ProSAT]</span></td></tr>
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[[Category: Dhe-Paganon, S.]]
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</table>
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[[Category: Dong, A.]]
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== Function ==
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[[Category: Edwards, A M.]]
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[https://www.uniprot.org/uniprot/HDAC6_HUMAN HDAC6_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.<ref>PMID:12024216</ref> <ref>PMID:17846173</ref> In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.<ref>PMID:12024216</ref> <ref>PMID:17846173</ref>
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[[Category: Kozieradzki, I.]]
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== Evolutionary Conservation ==
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[[Category: Li, Y.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Loppnau, P.]]
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Check<jmol>
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[[Category: MacKenzie, F.]]
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<jmolCheckbox>
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[[Category: Min, J.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/3c5k_consurf.spt"</scriptWhenChecked>
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[[Category: Ouyang, H.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Ravichandran, M.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: SGC, Structural Genomics Consortium.]]
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</jmolCheckbox>
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[[Category: Schuetz, A.]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3c5k ConSurf].
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[[Category: Weigelt, J.]]
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<div style="clear:both"></div>
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[[Category: ZN]]
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[[Category: actin-binding]]
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[[Category: chromatin regulator]]
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[[Category: cytoplasm]]
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[[Category: hdac6]]
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[[Category: hydrolase]]
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[[Category: metal-binding]]
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[[Category: nucleus]]
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[[Category: phosphoprotein]]
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[[Category: repressor]]
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[[Category: sgc]]
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[[Category: structural genomics]]
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[[Category: structural genomics consortium]]
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[[Category: transcription]]
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[[Category: transcription regulation]]
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[[Category: ubl conjugation]]
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[[Category: zinc finger]]
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[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:27 2008''
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==See Also==
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*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith CH]]
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[[Category: Bochkarev A]]
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[[Category: Bountra C]]
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[[Category: Dhe-Paganon S]]
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[[Category: Dong A]]
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[[Category: Edwards AM]]
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[[Category: Kozieradzki I]]
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[[Category: Li Y]]
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[[Category: Loppnau P]]
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[[Category: MacKenzie F]]
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[[Category: Min J]]
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[[Category: Ouyang H]]
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[[Category: Ravichandran M]]
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[[Category: Schuetz A]]
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[[Category: Weigelt J]]

Current revision

Crystal structure of human HDAC6 zinc finger domain

PDB ID 3c5k

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