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7d0q
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human HBO1-BRPF2 in complex with butyryl-coenzyme A== | |
| + | <StructureSection load='7d0q' size='340' side='right'caption='[[7d0q]], [[Resolution|resolution]] 2.21Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7d0q]] 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=7D0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D0Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</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=BCO:BUTYRYL+COENZYME+A'>BCO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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'>[https://proteopedia.org/fgij/fg.htm?mol=7d0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d0q OCA], [https://pdbe.org/7d0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d0q RCSB], [https://www.ebi.ac.uk/pdbsum/7d0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d0q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| - | + | ==See Also== | |
| - | + | *[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ding J]] | ||
| + | [[Category: Li W]] | ||
Current revision
Crystal structure of human HBO1-BRPF2 in complex with butyryl-coenzyme A
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