6ten: Difference between revisions

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'''Unreleased structure'''


The entry 6ten is ON HOLD  until Paper Publication
==Crystal structure of Dot1L in complex with an inhibitor (compound 11).==
 
<StructureSection load='6ten' size='340' side='right'caption='[[6ten]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ten]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TEN FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N5K:3-[(4-azanyl-6-methoxy-1,3,5-triazin-2-yl)amino]-4-[[(~{S})-[2,2-bis(fluoranyl)-1,3-benzodioxol-4-yl]-(3-chloranylpyridin-2-yl)methyl]amino]benzenesulfonamide'>N5K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6te6|6te6]], [[6tel|6tel]]</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=6ten FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ten OCA], [http://pdbe.org/6ten PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ten RCSB], [http://www.ebi.ac.uk/pdbsum/6ten PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ten 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]]