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==Crystal Structure of Human DOT1L in complex with inhibitor EPZ004777==
==Crystal Structure of Human DOT1L in complex with inhibitor EPZ004777==
<StructureSection load='4er3' size='340' side='right' caption='[[4er3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4er3' size='340' side='right'caption='[[4er3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4er3]] 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=4ER3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ER3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4er3]] 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=4ER3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ER3 FirstGlance]. <br>
</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eqz|4eqz]], [[4er0|4er0]], [[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=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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4er3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er3 OCA], [https://pdbe.org/4er3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4er3 RCSB], [https://www.ebi.ac.uk/pdbsum/4er3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4er3 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=4er3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er3 OCA], [http://pdbe.org/4er3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4er3 RCSB], [http://www.ebi.ac.uk/pdbsum/4er3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4er3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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==
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</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: Scopton A]]
[[Category: Scopton, A]]
[[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]]

Latest revision as of 14:05, 1 March 2024

Crystal Structure of Human DOT1L in complex with inhibitor EPZ004777Crystal Structure of Human DOT1L in complex with inhibitor EPZ004777

Structural highlights

4er3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DOT1L_HUMAN Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.

See Also

4er3, resolution 2.40Å

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