4er3: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4er3]] is a 1 chain structure with sequence from [http://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 [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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ER3 FirstGlance]. <br>
</td></tr><tr><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><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>
<tr><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='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><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 Homo sapiens])</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 Homo sapiens])</td></tr>
<tr><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='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><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://www.rcsb.org/pdb/explore.do?structureId=4er3 RCSB], [http://www.ebi.ac.uk/pdbsum/4er3 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=4er3 RCSB], [http://www.ebi.ac.uk/pdbsum/4er3 PDBsum]</span></td></tr>
<table>
</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.


==See Also==
==See Also==
Line 16: Line 18:
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C.]]
[[Category: Bountra, C]]
[[Category: Bradner, J E.]]
[[Category: Bradner, J E]]
[[Category: Brown, P J.]]
[[Category: Brown, P J]]
[[Category: Edwards, A M.]]
[[Category: Edwards, A M]]
[[Category: Federation, A.]]
[[Category: Federation, A]]
[[Category: Li, Y.]]
[[Category: Li, Y]]
[[Category: Marineau, J.]]
[[Category: Marineau, J]]
[[Category: Nguyen, K T.]]
[[Category: Nguyen, K T]]
[[Category: Qi, J.]]
[[Category: Qi, J]]
[[Category: SGC, Structural Genomics Consortium.]]
[[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, A K.]]
[[Category: Wernimont, A K]]
[[Category: Yu, W.]]
[[Category: Yu, W]]
[[Category: Epigenetic]]
[[Category: Epigenetic]]
[[Category: Histone]]
[[Category: Histone]]
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Transferase-transferase inhibitor complex]]
[[Category: Transferase-transferase inhibitor complex]]

Revision as of 17:00, 25 December 2014

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.
Ligands:, , ,
Gene:DOT1L, KIAA1814, KMT4 (Homo sapiens)
Activity:Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:FirstGlance, OCA, RCSB, PDBsum

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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