6tel: Difference between revisions

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-'''Unreleased structure'''
-The entry 6tel is ON HOLD  until Paper Publication
+==Crystal structure of Dot1L in complex with an inhibitor (compound 10).==
+<StructureSection load='6tel' size='340' side='right'caption='[[6tel]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6tel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TEL FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=N4Z:~{N}1-[(~{S})-[2,2-bis(fluoranyl)-1,3-benzodioxol-4-yl]-(3-chloranylpyridin-2-yl)methyl]-~{N}2-(4-methoxy-6-piperazin-1-yl-1,3,5-triazin-2-yl)-4-methylsulfonyl-benzene-1,2-diamine'>N4Z</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6te6|6te6]]</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=6tel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tel OCA], [http://pdbe.org/6tel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tel RCSB], [http://www.ebi.ac.uk/pdbsum/6tel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tel ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DOT1L_HUMAN DOT1L_HUMAN]] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.
+__TOC__
+</StructureSection>
+[[Category: Histone-lysine N-methyltransferase]]
+[[Category: Large Structures]]
+[[Category: Be, C]]
+[[Category: Moebitz, H]]
+[[Category: Scheufler, C]]
+[[Category: Stauffer, F]]
+[[Category: Complex structure]]
+[[Category: Dot1l]]
+[[Category: Inhibitor]]
+[[Category: Transferase]]