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3f2k

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==Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR==
==Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR==
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<StructureSection load='3f2k' size='340' side='right' caption='[[3f2k]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='3f2k' size='340' side='right'caption='[[3f2k]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3f2k]] is a 3 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=3F2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F2K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3f2k]] is a 3 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=3F2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F2K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETMAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f2k OCA], [https://pdbe.org/3f2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f2k RCSB], [https://www.ebi.ac.uk/pdbsum/3f2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f2k ProSAT]</span></td></tr>
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<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>
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<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=3f2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f2k RCSB], [http://www.ebi.ac.uk/pdbsum/3f2k PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/3f2k_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/3f2k_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=3f2k ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Histone methyltransferase|Histone methyltransferase]]
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Amaya, M F]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Amaya MF]]
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[[Category: Botchkarev, A]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Botchkarev A]]
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[[Category: Dombrovski, L]]
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[[Category: Bountra C]]
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[[Category: Edwards, A M]]
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[[Category: Dombrovski L]]
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[[Category: Min, J]]
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[[Category: Edwards AM]]
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[[Category: Ni, S]]
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[[Category: Min J]]
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[[Category: Plotnikov, A N]]
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[[Category: Ni S]]
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[[Category: Structural genomic]]
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[[Category: Plotnikov AN]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Wu, H]]
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[[Category: Wu H]]
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[[Category: Chromatin regulator]]
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[[Category: Dna damage]]
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[[Category: Dna repair]]
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[[Category: Dna-binding]]
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[[Category: Histone-lysine n-methyltransferase setmar]]
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[[Category: Methyltransferase]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Set domain and mariner transposase fusion]]
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[[Category: Set domain and mariner transposase fusion gene-containing protein]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR

PDB ID 3f2k

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