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==Crystal structure of Dot1L in complex with inhibitor CPD2 [2-(2-(5-((2-chlorophenoxy)methyl)-1H-tetrazol-1-yl)acetyl)-N-(4-chlorophenyl)hydrazinecarboxamide]== | |||
<StructureSection load='5drt' size='340' side='right' caption='[[5drt]], [[Resolution|resolution]] 2.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5drt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DRT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5EG:2-({5-[(2-CHLOROPHENOXY)METHYL]-1H-TETRAZOL-1-YL}ACETYL)-N-(4-CHLOROPHENYL)HYDRAZINECARBOXAMIDE'>5EG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=5drt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5drt OCA], [http://pdbe.org/5drt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5drt RCSB], [http://www.ebi.ac.uk/pdbsum/5drt PDBsum]</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: Gaul, C]] | |||
[[Category: Moebitz, H]] | |||
[[Category: Scheufler, C]] | |||
[[Category: Complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Methyltransferase]] | |||
[[Category: Transferase]] | |||
Revision as of 01:23, 21 June 2016
Crystal structure of Dot1L in complex with inhibitor CPD2 [2-(2-(5-((2-chlorophenoxy)methyl)-1H-tetrazol-1-yl)acetyl)-N-(4-chlorophenyl)hydrazinecarboxamide]Crystal structure of Dot1L in complex with inhibitor CPD2 [2-(2-(5-((2-chlorophenoxy)methyl)-1H-tetrazol-1-yl)acetyl)-N-(4-chlorophenyl)hydrazinecarboxamide]
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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