3bo5: Difference between revisions

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[[Image:3bo5.jpg|left|200px]]<br /><applet load="3bo5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3bo5, resolution 1.59&Aring;" />
'''Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR'''<br />


==About this Structure==
==Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR==
3BO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BO5 OCA].  
<StructureSection load='3bo5' size='340' side='right'caption='[[3bo5]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
[[Category: Histone-lysine N-methyltransferase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[3bo5]] 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=3BO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BO5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3bo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bo5 OCA], [https://pdbe.org/3bo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bo5 RCSB], [https://www.ebi.ac.uk/pdbsum/3bo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bo5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SETMR_HUMAN SETMR_HUMAN] Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'. Has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element. Has DNA nicking activity. Has in vivo end joining activity and may mediate genomic integration of foreign DNA.<ref>PMID:16332963</ref> <ref>PMID:16672366</ref> <ref>PMID:17877369</ref> <ref>PMID:17403897</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3bo5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bo5 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Bochkarev, A.]]
[[Category: Bochkarev A]]
[[Category: Dobrovetsky, E.]]
[[Category: Dobrovetsky E]]
[[Category: Edwards, A M.]]
[[Category: Edwards AM]]
[[Category: Lunin, V V.]]
[[Category: Lunin VV]]
[[Category: Min, J.]]
[[Category: Min J]]
[[Category: Plotnikov, A N.]]
[[Category: Plotnikov AN]]
[[Category: Ren, H.]]
[[Category: Ren H]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Weigelt J]]
[[Category: Weigelt, J.]]
[[Category: Wu H]]
[[Category: Wu, H.]]
[[Category: GOL]]
[[Category: SAH]]
[[Category: ZN]]
[[Category: alternative splicing]]
[[Category: chromatin regulator]]
[[Category: coiled coil]]
[[Category: dna damage]]
[[Category: dna repair]]
[[Category: dna-binding]]
[[Category: methyltransferase]]
[[Category: nucleus]]
[[Category: set domain]]
[[Category: setmar]]
[[Category: sgc]]
[[Category: structural genomics]]
[[Category: structural genomics consortium]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:06:43 2008''
Retrieved from "https://proteopedia.org/3bo5"