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==Crystal structure of human HBO1 in complex with BRPF2==
==Crystal structure of human HBO1 in complex with BRPF2==
<StructureSection load='5gk9' size='340' side='right' caption='[[5gk9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5gk9' size='340' side='right'caption='[[5gk9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5gk9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GK9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5gk9]] 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=5GK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GK9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAT7, HBO1, HBOa, MYST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BRD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=5gk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk9 OCA], [https://pdbe.org/5gk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gk9 RCSB], [https://www.ebi.ac.uk/pdbsum/5gk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gk9 OCA], [http://pdbe.org/5gk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gk9 RCSB], [http://www.ebi.ac.uk/pdbsum/5gk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gk9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KAT7_HUMAN KAT7_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. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1 (PubMed:18832067). Specifically represses AR-mediated transcription.<ref>PMID:10438470</ref> <ref>PMID:10930412</ref> <ref>PMID:11278932</ref> <ref>PMID:16387653</ref> <ref>PMID:18832067</ref>
[https://www.uniprot.org/uniprot/KAT7_HUMAN KAT7_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. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1 (PubMed:18832067). Specifically represses AR-mediated transcription.<ref>PMID:10438470</ref> <ref>PMID:10930412</ref> <ref>PMID:11278932</ref> <ref>PMID:16387653</ref> <ref>PMID:18832067</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5gk9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5gk9" style="background-color:#fffaf0;"></div>
==See Also==
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Ding, J]]
[[Category: Ding J]]
[[Category: Tao, Y]]
[[Category: Tao Y]]
[[Category: Xu, S]]
[[Category: Xu S]]
[[Category: Zhu, J]]
[[Category: Zhu J]]
[[Category: Hat]]
[[Category: Transferase-metal binding protein complex]]
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