3c6w

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Current revision (22:32, 26 March 2025) (edit) (undo)
 
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<StructureSection load='3c6w' size='340' side='right'caption='[[3c6w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='3c6w' size='340' side='right'caption='[[3c6w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3c6w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6W FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3c6w]] is a 4 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=3C6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6W FirstGlance]. <br>
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</td></tr><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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></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=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ING5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3c6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6w OCA], [https://pdbe.org/3c6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6w RCSB], [https://www.ebi.ac.uk/pdbsum/3c6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6w 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=3c6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6w OCA], [https://pdbe.org/3c6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6w RCSB], [https://www.ebi.ac.uk/pdbsum/3c6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ING5_HUMAN ING5_HUMAN]] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator.<ref>PMID:12750254</ref> <ref>PMID:16387653</ref>
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[https://www.uniprot.org/uniprot/ING5_HUMAN ING5_HUMAN] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator.<ref>PMID:12750254</ref> <ref>PMID:16387653</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/3c6w_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/3c6w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Champagne, K S]]
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[[Category: Champagne KS]]
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[[Category: Johnson, K]]
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[[Category: Johnson K]]
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[[Category: Kutateladze, T G]]
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[[Category: Kutateladze TG]]
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[[Category: Pena, P V]]
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[[Category: Pena PV]]
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[[Category: Alternative splicing]]
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[[Category: Chromatin]]
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[[Category: Epigenetic]]
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[[Category: Histone]]
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[[Category: Ing]]
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[[Category: Metal binding protein]]
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[[Category: Metal-binding]]
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[[Category: Phd]]
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[[Category: Phosphoprotein]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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Current revision

Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptide

PDB ID 3c6w

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