4hra: Difference between revisions

No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal Structure of DOT1L in Complex with EPZ-5676==
==Crystal Structure of DOT1L in Complex with EPZ-5676==
<StructureSection load='4hra' size='340' side='right' caption='[[4hra]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
<StructureSection load='4hra' size='340' side='right'caption='[[4hra]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4hra]] 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=4HRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HRA FirstGlance]. <br>
<table><tr><td colspan='2'>[[4hra]] 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=4HRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HRA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EP6:5-[{CIS-3-[2-(5-TERT-BUTYL-1H-BENZIMIDAZOL-2-YL)ETHYL]CYCLOBUTYL}(PROPAN-2-YL)AMINO]-5-DEOXYADENOSINE'>EP6</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ekg|4ekg]], [[4eki|4eki]], [[4ek9|4ek9]], [[3qow|3qow]], [[3qox|3qox]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP6:5-[{CIS-3-[2-(5-TERT-BUTYL-1H-BENZIMIDAZOL-2-YL)ETHYL]CYCLOBUTYL}(PROPAN-2-YL)AMINO]-5-DEOXYADENOSINE'>EP6</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hra OCA], [https://pdbe.org/4hra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hra RCSB], [https://www.ebi.ac.uk/pdbsum/4hra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hra 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=4hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hra OCA], [http://pdbe.org/4hra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hra RCSB], [http://www.ebi.ac.uk/pdbsum/4hra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hra 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 23: Line 21:


==See Also==
==See Also==
*[[Histone methyltransferase|Histone methyltransferase]]
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Jin, L]]
[[Category: Jin L]]
[[Category: Histone lysine methyltransferase]]
[[Category: Transferase]]
[[Category: Transferase-transferase inhibitor complex]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA