2p0w: Difference between revisions

<StructureSection load='2p0w' size='340' side='right'caption='[[2p0w]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

== Structural highlights ==

<table><tr><td colspan='2'>[[2p0w]] is a 4 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=2P0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P0W 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]] 1.9&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p0w OCA], [https://pdbe.org/2p0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p0w RCSB], [https://www.ebi.ac.uk/pdbsum/2p0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p0w ProSAT]</span></td></tr>

== Function ==

[https://www.uniprot.org/uniprot/HAT1_HUMAN HAT1_HUMAN] Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.<ref>PMID:9427644</ref> <ref>PMID:11585814</ref> <ref>PMID:20953179</ref>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/2p0w_consurf.spt"</scriptWhenChecked>

    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>

    <text>to colour the structure by Evolutionary Conservation</text>

  </jmolCheckbox>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p0w ConSurf].

<div style="clear:both"></div>

==See Also==

*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: Arrowsmith CH]]

[[Category: Bochkarev A]]

[[Category: Edwards AM]]

[[Category: Loppnau P]]

[[Category: Min J]]

[[Category: Plotnikov AN]]

[[Category: Sundstrom M]]

[[Category: Weigelt J]]

[[Category: Wu H]]

[[Category: Zeng H]]