5ttf: Difference between revisions

<StructureSection load='5ttf' size='340' side='right'caption='[[5ttf]], [[Resolution|resolution]] 1.72&Aring;' scene=''>

<table><tr><td colspan='2'>[[5ttf]] 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=5TTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TTF 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]] 1.72&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7KZ:N4-(1-METHYLPIPERIDIN-4-YL)-N2-HEXYL-6,7-DIMETHOXYQUINAZOLINE-2,4-DIAMINE'>7KZ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=5ttf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttf OCA], [https://pdbe.org/5ttf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ttf RCSB], [https://www.ebi.ac.uk/pdbsum/5ttf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttf ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref>  

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

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Arrowsmith CH]]

[[Category: BABAULT N]]

[[Category: BROWN PJ]]

[[Category: Bountra C]]

[[Category: DONG A]]

[[Category: Edwards AM]]

[[Category: JIN J]]

[[Category: LIU J]]

[[Category: TEMPEL W]]

[[Category: WU H]]

[[Category: XIONG Y]]

[[Category: ZENG H]]