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==Crystal structure of Dot1L in complex with inhibitor CPD7 [N-(3-(((R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-yl)(methyl)amino)propyl)-2-(3-(2-chloro-3-(2-methylpyridin-3-yl)benzo[b]thiophen-5-yl)ureido)acetamide]== | |||
<StructureSection load='5mw4' size='340' side='right' caption='[[5mw4]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mw4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MW4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5JU:N~2~-{[2-CHLORO-3-(2-METHYLPYRIDIN-3-YL)-1-BENZOTHIOPHEN-5-YL]CARBAMOYL}-N-(3-{METHYL[(3R)-1-(5H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)PIPERIDIN-3-YL]AMINO}PROPYL)GLYCINAMIDE'>5JU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
[[Category: | <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=5mw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mw4 OCA], [http://pdbe.org/5mw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mw4 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: Be, C]] | [[Category: Be, C]] | ||
[[Category: Gaul, C]] | [[Category: Gaul, C]] | ||
[[Category: Koch, E]] | |||
[[Category: Moebitz, H]] | [[Category: Moebitz, H]] | ||
[[Category: Scheufler, C]] | |||
[[Category: Stauffer, F]] | [[Category: Stauffer, F]] | ||
[[Category: | [[Category: Complex]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: Methyltransferase]] | |||
[[Category: Transferase]] | |||
Revision as of 19:24, 22 March 2017
Crystal structure of Dot1L in complex with inhibitor CPD7 [N-(3-(((R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-yl)(methyl)amino)propyl)-2-(3-(2-chloro-3-(2-methylpyridin-3-yl)benzo[b]thiophen-5-yl)ureido)acetamide]Crystal structure of Dot1L in complex with inhibitor CPD7 [N-(3-(((R)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-3-yl)(methyl)amino)propyl)-2-(3-(2-chloro-3-(2-methylpyridin-3-yl)benzo[b]thiophen-5-yl)ureido)acetamide]
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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