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1vkg

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==Crystal Structure of Human HDAC8 complexed with CRA-19156==
==Crystal Structure of Human HDAC8 complexed with CRA-19156==
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<StructureSection load='1vkg' size='340' side='right' caption='[[1vkg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='1vkg' size='340' side='right'caption='[[1vkg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1vkg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VKG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1vkg]] 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=1VKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VKG FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRI:5-(4-METHYL-BENZOYLAMINO)-BIPHENYL-3,4-DICARBOXYLIC+ACID+3-DIMETHYLAMIDE-4-HYDROXYAMIDE'>CRI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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]] 2.2&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t64|1t64]], [[1t67|1t67]], [[1t69|1t69]]</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=CRI:5-(4-METHYL-BENZOYLAMINO)-BIPHENYL-3,4-DICARBOXYLIC+ACID+3-DIMETHYLAMIDE-4-HYDROXYAMIDE'>CRI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vkg OCA], [https://pdbe.org/1vkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vkg RCSB], [https://www.ebi.ac.uk/pdbsum/1vkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vkg ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vkg RCSB], [http://www.ebi.ac.uk/pdbsum/1vkg PDBsum]</span></td></tr>
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</table>
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/1vkg_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/1vkg_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1vkg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1vkg" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Histone deacetylase|Histone deacetylase]]
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*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arvai, A.]]
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[[Category: Large Structures]]
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[[Category: Buggy, J J.]]
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[[Category: Arvai A]]
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[[Category: Chi, E.]]
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[[Category: Buggy JJ]]
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[[Category: Dougan, D R.]]
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[[Category: Chi E]]
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[[Category: Ho, J D.]]
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[[Category: Dougan DR]]
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[[Category: Jennings, A J.]]
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[[Category: Ho JD]]
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[[Category: Katz, B A.]]
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[[Category: Jennings AJ]]
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[[Category: Knuth, M W.]]
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[[Category: Katz BA]]
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[[Category: Leahy, E M.]]
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[[Category: Knuth MW]]
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[[Category: Luong, C.]]
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[[Category: Leahy EM]]
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[[Category: McRee, D E.]]
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[[Category: Luong C]]
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[[Category: Mol, C.]]
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[[Category: McRee DE]]
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[[Category: Navre, M.]]
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[[Category: Mol C]]
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[[Category: Sang, B C.]]
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[[Category: Navre M]]
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[[Category: Skene, R J.]]
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[[Category: Sang B-C]]
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[[Category: Snell, G.]]
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[[Category: Skene RJ]]
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[[Category: Somoza, J R.]]
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[[Category: Snell G]]
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[[Category: Swanson, R V.]]
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[[Category: Somoza JR]]
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[[Category: Tang, J.]]
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[[Category: Swanson RV]]
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[[Category: Tari, L W.]]
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[[Category: Tang J]]
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[[Category: Verner, E.]]
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[[Category: Tari LW]]
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[[Category: Wynands, R.]]
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[[Category: Verner E]]
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[[Category: Histone deacetylase]]
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[[Category: Wynands R]]
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[[Category: Hydrolase]]
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[[Category: Zinc hydrolase]]
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Current revision

Crystal Structure of Human HDAC8 complexed with CRA-19156

PDB ID 1vkg

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