6tel: Difference between revisions
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==Crystal structure of Dot1L in complex with an inhibitor (compound 10).== | |||
<StructureSection load='6tel' size='340' side='right'caption='[[6tel]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
== 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> | |||
</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: | <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]] | |||
Revision as of 18:24, 11 December 2019
Crystal structure of Dot1L in complex with an inhibitor (compound 10).Crystal structure of Dot1L in complex with an inhibitor (compound 10).
Structural highlights
Function[DOT1L_HUMAN] Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA. |
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