6oiq: Difference between revisions
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==Crystal structure of MYST acetyltransferase domain in complex with inhibitor 63== | |||
<StructureSection load='6oiq' size='340' side='right'caption='[[6oiq]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oiq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OIQ FirstGlance]. <br> | |||
</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=MLV:2-fluoro-N-(phenylsulfonyl)[1,1-biphenyl]-3-carbohydrazide'>MLV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
[[Category: | <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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6oiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oiq OCA], [http://pdbe.org/6oiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oiq RCSB], [http://www.ebi.ac.uk/pdbsum/6oiq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oiq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Histone acetyltransferase]] | |||
[[Category: Large Structures]] | |||
[[Category: Baell, J B]] | |||
[[Category: Chung, M C]] | |||
[[Category: Hermans, S J]] | |||
[[Category: Parker, M W]] | |||
[[Category: Thomas, T]] | [[Category: Thomas, T]] | ||
[[Category: | [[Category: Complex]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: | [[Category: Myst]] | ||
[[Category: | [[Category: Transferase]] | ||
[[Category: Transferase-transferase inhibitor complex]] | |||
Revision as of 05:58, 3 July 2019
Crystal structure of MYST acetyltransferase domain in complex with inhibitor 63
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