6owi

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<StructureSection load='6owi' size='340' side='right'caption='[[6owi]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='6owi' size='340' side='right'caption='[[6owi]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6owi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OWI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6owi]] is a 1 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=6OWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OWI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NB7:N-[(2-fluorophenyl)sulfonyl]benzohydrazide'>NB7</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.75&#8491;</td></tr>
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<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>
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<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NB7:N-[(2-fluorophenyl)sulfonyl]benzohydrazide'>NB7</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6owi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owi OCA], [https://pdbe.org/6owi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6owi RCSB], [https://www.ebi.ac.uk/pdbsum/6owi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6owi ProSAT]</span></td></tr>
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<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=6owi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owi OCA], [http://pdbe.org/6owi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6owi RCSB], [http://www.ebi.ac.uk/pdbsum/6owi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6owi ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KAT8_HUMAN KAT8_HUMAN]] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.<ref>PMID:12397079</ref> <ref>PMID:15923642</ref> <ref>PMID:20018852</ref>
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[https://www.uniprot.org/uniprot/KAT8_HUMAN KAT8_HUMAN] Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.<ref>PMID:12397079</ref> <ref>PMID:15923642</ref> <ref>PMID:20018852</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 6owi" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6owi" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baell, J B]]
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[[Category: Baell JB]]
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[[Category: Chung, M C]]
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[[Category: Chung MC]]
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[[Category: Hermans, S J]]
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[[Category: Hermans SJ]]
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[[Category: Parker, M W]]
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[[Category: Parker MW]]
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[[Category: Thomas, T]]
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[[Category: Thomas T]]
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[[Category: Complex]]
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[[Category: Inhibitor]]
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[[Category: Myst]]
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[[Category: Transferase]]
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[[Category: Transferase-transerase inhibitor complex]]
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Current revision

Crystal structure of MYST acetyltransferase domain in complex with inhibitor 85

PDB ID 6owi

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