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4er5

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==Crystal structure of human DOT1L in complex with 2 molecules of EPZ004777==
==Crystal structure of human DOT1L in complex with 2 molecules of EPZ004777==
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<StructureSection load='4er5' size='340' side='right' caption='[[4er5]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
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<StructureSection load='4er5' size='340' side='right'caption='[[4er5]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4er5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ER5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4er5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ER5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QK:7-{5-[(3-{[(4-TERT-BUTYLPHENYL)CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]-5-DEOXY-BETA-D-RIBOFURANOSYL}-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>0QK</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eqz|4eqz]], [[4er0|4er0]], [[4er3|4er3]], [[4er6|4er6]], [[4er7|4er7]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QK:7-{5-[(3-{[(4-TERT-BUTYLPHENYL)CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]-5-DEOXY-BETA-D-RIBOFURANOSYL}-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE'>0QK</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DOT1L, KIAA1814, KMT4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4er5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er5 OCA], [https://pdbe.org/4er5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4er5 RCSB], [https://www.ebi.ac.uk/pdbsum/4er5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4er5 ProSAT]</span></td></tr>
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<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>
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<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=4er5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er5 OCA], [http://pdbe.org/4er5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4er5 RCSB], [http://www.ebi.ac.uk/pdbsum/4er5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4er5 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
==See Also==
==See Also==
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*[[Histone methyltransferase|Histone methyltransferase]]
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Bradner, J E]]
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[[Category: Bradner JE]]
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[[Category: Brown, P J]]
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[[Category: Brown PJ]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Federation, A]]
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[[Category: Federation A]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Marineau, J]]
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[[Category: Marineau J]]
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[[Category: Nguyen, K T]]
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[[Category: Nguyen KT]]
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[[Category: Qi, J]]
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[[Category: Qi J]]
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[[Category: Structural genomic]]
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[[Category: Schapira M]]
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[[Category: Schapira, M]]
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[[Category: Scopton A]]
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[[Category: Scopton, A]]
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[[Category: Tempel W]]
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[[Category: Tempel, W]]
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[[Category: Vedadi M]]
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[[Category: Vedadi, M]]
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[[Category: Wernimont AK]]
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[[Category: Wernimont, A K]]
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[[Category: Yu W]]
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[[Category: Yu, W]]
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[[Category: Epigenetic]]
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[[Category: Histone]]
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[[Category: Methyltransferase]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Crystal structure of human DOT1L in complex with 2 molecules of EPZ004777

PDB ID 4er5

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