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4eqz

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Crystal structure of human DOT1L in complex with inhibitor FED2

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Retrieved from "http://52.214.119.220/wiki/index.php/4eqz"

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 ==Crystal structure of human DOT1L in complex with inhibitor FED2==
-<StructureSection load='4eqz' size='340' side='right' caption='[[4eqz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+<StructureSection load='4eqz' size='340' side='right'caption='[[4eqz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4eqz]] 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=4EQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EQZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4eqz]] 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=4EQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EQZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AW0:5-DEOXY-5-[(3-{[(4-METHYLPHENYL)CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]ADENOSINE'>AW0</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4er0|4er0]], [[4er3|4er3]], [[4er5|4er5]], [[4er6|4er6]], [[4er7|4er7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AW0:5-DEOXY-5-[(3-{[(4-METHYLPHENYL)CARBAMOYL]AMINO}PROPYL)(PROPAN-2-YL)AMINO]ADENOSINE'>AW0</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eqz OCA], [https://pdbe.org/4eqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eqz RCSB], [https://www.ebi.ac.uk/pdbsum/4eqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eqz ProSAT]</span></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=4eqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eqz OCA], [http://pdbe.org/4eqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eqz RCSB], [http://www.ebi.ac.uk/pdbsum/4eqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eqz 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.
+[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==
-*[[Histone methyltransferase|Histone methyltransferase]]
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Histone-lysine N-methyltransferase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Bradner, J E]]
+[[Category: Bradner JE]]
-[[Category: Brown, P J]]
+[[Category: Brown PJ]]
-[[Category: Edwards, A M]]
+[[Category: Edwards AM]]
-[[Category: Federation, A]]
+[[Category: Federation A]]
-[[Category: Li, Y]]
+[[Category: Li Y]]
-[[Category: Marineau, J]]
+[[Category: Marineau J]]
-[[Category: Nguyen, K T]]
+[[Category: Nguyen KT]]
-[[Category: Qi, J]]
+[[Category: Qi J]]
-[[Category: Structural genomic]]
+[[Category: Schapira M]]
-[[Category: Schapira, M]]
+[[Category: Tempel W]]
-[[Category: Tempel, W]]
+[[Category: Vedadi M]]
-[[Category: Vedadi, M]]
+[[Category: Wernimont AK]]
-[[Category: Wernimont, A K]]
+[[Category: Yu W]]
-[[Category: Yu, W]]
-[[Category: Epigenetic]]
-[[Category: Histone]]
-[[Category: Methyltransferase]]
-[[Category: Transferase-transferase inhibitor complex]]

4eqz

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Current revision

Crystal structure of human DOT1L in complex with inhibitor FED2

Structural highlights

Function

See Also

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