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5fcw

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'''Unreleased structure'''
 
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The entry 5fcw is ON HOLD until Paper Publication
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==HDAC8 Complexed with a Hydroxamic Acid==
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<StructureSection load='5fcw' size='340' side='right'caption='[[5fcw]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5fcw]] is a 2 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=5FCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FCW FirstGlance]. <br>
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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]] 1.979&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5YA:4-NAPHTHALEN-1-YL-~{N}-OXIDANYL-BENZAMIDE'>5YA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=5fcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcw OCA], [https://pdbe.org/5fcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fcw RCSB], [https://www.ebi.ac.uk/pdbsum/5fcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
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Authors: Cole, K.E., Perry, K.
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==See Also==
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*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
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Description: HDAC8 Complexed with a Hydroxamic Acid
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Perry, K]]
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__TOC__
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[[Category: Cole, K.E]]
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cole KE]]
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[[Category: Perry K]]

Current revision

HDAC8 Complexed with a Hydroxamic Acid

PDB ID 5fcw

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