3bo5

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Current revision (09:30, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3bo5' size='340' side='right'caption='[[3bo5]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
<StructureSection load='3bo5' size='340' side='right'caption='[[3bo5]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bo5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
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<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>
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</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>
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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]] 1.59&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETMAR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://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'>[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>
<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>
</table>
== Function ==
== Function ==
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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>
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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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone-lysine N-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Dobrovetsky, E]]
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[[Category: Dobrovetsky E]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Lunin, V V]]
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[[Category: Lunin VV]]
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[[Category: Min, J]]
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[[Category: Min J]]
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[[Category: Plotnikov, A N]]
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[[Category: Plotnikov AN]]
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[[Category: Ren, H]]
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[[Category: Ren H]]
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[[Category: Structural genomic]]
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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: Methyltransferase]]
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[[Category: Nucleus]]
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[[Category: Set domain]]
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[[Category: Setmar]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR

PDB ID 3bo5

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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