3c6w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 3: Line 3:
<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 ==
<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>
<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>
</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>
</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>
<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>
<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>
<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>
<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 ==
[[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>
[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]]
Line 16: Line 15:
   <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <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>
Line 25: Line 24:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Champagne, K S]]
[[Category: Champagne KS]]
[[Category: Johnson, K]]
[[Category: Johnson K]]
[[Category: Kutateladze, T G]]
[[Category: Kutateladze TG]]
[[Category: Pena, P V]]
[[Category: Pena PV]]
[[Category: Alternative splicing]]
[[Category: Chromatin]]
[[Category: Epigenetic]]
[[Category: Histone]]
[[Category: Ing]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]
[[Category: Phd]]
[[Category: Phosphoprotein]]
[[Category: Zinc]]
[[Category: Zinc-finger]]

Latest revision as of 22:32, 26 March 2025

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

3c6w, resolution 1.75Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA