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3smt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3smt is ON HOLD Authors: Dong, A., Zeng, H., Walker, J.R., Loppnau, P., Bountra, C., Weigelt, J., Arrowsmith, C.H., Edwards, A.M., Min, J., Wu, H., ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human SET domain-containing protein3== | |
| + | <StructureSection load='3smt' size='340' side='right'caption='[[3smt]], [[Resolution|resolution]] 2.04Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3smt]] 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=3SMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SMT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ARS:ARSENIC'>ARS</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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">SETD3, C14orf154 ([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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3smt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3smt OCA], [https://pdbe.org/3smt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3smt RCSB], [https://www.ebi.ac.uk/pdbsum/3smt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3smt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/SETD3_HUMAN SETD3_HUMAN]] Histone methyltransferase that methylates 'Lys-36' of histone H3 (H3K36me). H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). | ||
| - | + | ==See Also== | |
| - | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Histone-lysine N-methyltransferase]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bountra, C]] | ||
| + | [[Category: Dong, A]] | ||
| + | [[Category: Edwards, A M]] | ||
| + | [[Category: Loppnau, P]] | ||
| + | [[Category: Min, J]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Walker, J R]] | ||
| + | [[Category: Weigelt, J]] | ||
| + | [[Category: Wu, H]] | ||
| + | [[Category: Zeng, H]] | ||
| + | [[Category: Histone methyltransferase]] | ||
| + | [[Category: Histone modification]] | ||
| + | [[Category: Lysine]] | ||
| + | [[Category: Post-translational modification]] | ||
| + | [[Category: Setd3]] | ||
| + | [[Category: Sgc]] | ||
| + | [[Category: Transferase]] | ||
Current revision
Crystal structure of human SET domain-containing protein3
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Arrowsmith, C H | Bountra, C | Dong, A | Edwards, A M | Loppnau, P | Min, J | Structural genomic | Walker, J R | Weigelt, J | Wu, H | Zeng, H | Histone methyltransferase | Histone modification | Lysine | Post-translational modification | Setd3 | Sgc | Transferase
