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3d7c

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Current revision (12:42, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3d7c' size='340' side='right'caption='[[3d7c]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
<StructureSection load='3d7c' size='340' side='right'caption='[[3d7c]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3d7c]] is a 2 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=3D7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D7C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3d7c]] 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=3D7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D7C FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GCN5L2, GCN5, HGCN5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.06&#8491;</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=3d7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d7c OCA], [https://pdbe.org/3d7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d7c RCSB], [https://www.ebi.ac.uk/pdbsum/3d7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d7c 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=3d7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d7c OCA], [https://pdbe.org/3d7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d7c RCSB], [https://www.ebi.ac.uk/pdbsum/3d7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d7c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KAT2A_HUMAN KAT2A_HUMAN]] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non-histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.<ref>PMID:17301242</ref> <ref>PMID:19103755</ref>
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[https://www.uniprot.org/uniprot/KAT2A_HUMAN KAT2A_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non-histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.<ref>PMID:17301242</ref> <ref>PMID:19103755</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Eswaran J]]
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[[Category: Eswaran, J]]
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[[Category: Fedorov O]]
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[[Category: Fedorov, O]]
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[[Category: Filippakopoulos P]]
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[[Category: Filippakopoulos, P]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Murray J]]
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[[Category: Murray, J]]
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[[Category: Picaud S]]
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[[Category: Picaud, S]]
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[[Category: Von Delft F]]
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[[Category: Structural genomic]]
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[[Category: Amino-acid synthesis]]
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[[Category: Biosynthetic protein]]
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[[Category: Bromodomain]]
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[[Category: Gcn5]]
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[[Category: Host-virus interaction]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the bromodomain of human GCN5, the general control of amino-acid synthesis protein 5-like 2

PDB ID 3d7c

Drag the structure with the mouse to rotate

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OCA

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