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3f2k
From Proteopedia
(Difference between revisions)
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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== | ||
| - | <StructureSection load='3f2k' size='340' side='right' caption='[[3f2k]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='3f2k' size='340' side='right'caption='[[3f2k]], [[Resolution|resolution]] 1.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3f2k]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3f2k]] is a 3 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=3F2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F2K FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
<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> | <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> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETMAR ([ | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 24: | Line 24: | ||
==See Also== | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 31: | Line 31: | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Amaya, M F]] | [[Category: Amaya, M F]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 09:22, 23 February 2022
Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Amaya, M F | Arrowsmith, C H | Botchkarev, A | Bountra, C | Dombrovski, L | Edwards, A M | Min, J | Ni, S | Plotnikov, A N | Structural genomic | Weigelt, J | Wu, H | Alternative splicing | Chromatin regulator | Coiled coil | Dna damage | Dna repair | Dna-binding | Histone-lysine n-methyltransferase setmar | Methyltransferase | Nucleus | Phosphoprotein | Set domain and mariner transposase fusion | Set domain and mariner transposase fusion gene-containing protein | Sgc | Transferase
