5wxg: Difference between revisions

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<StructureSection load='5wxg' size='340' side='right'caption='[[5wxg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='5wxg' size='340' side='right'caption='[[5wxg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5wxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WXG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WXG FirstGlance]. <br>
<table><tr><td colspan='2'>[[5wxg]] 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=5WXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WXG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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]] 1.703&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wxg OCA], [http://pdbe.org/5wxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wxg RCSB], [http://www.ebi.ac.uk/pdbsum/5wxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wxg 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=5wxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wxg OCA], [https://pdbe.org/5wxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wxg RCSB], [https://www.ebi.ac.uk/pdbsum/5wxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wxg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TAF3_HUMAN TAF3_HUMAN]] Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.  
[https://www.uniprot.org/uniprot/TAF3_HUMAN TAF3_HUMAN] Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Zhao, S]]
[[Category: Zhao S]]
[[Category: Histone h3]]
[[Category: Hydrolase]]
[[Category: Taf3]]

Latest revision as of 04:56, 21 November 2024

Structure of TAF PHD finger domain binds to H3(1-15)K4ac

5wxg, resolution 1.70Å

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