This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3mek
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine== | ==Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine== | ||
<StructureSection load='3mek' size='340' side='right' caption='[[3mek]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3mek' size='340' side='right' caption='[[3mek]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3mek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3mek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MEK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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">SMYD3, ZMYND1, ZNFN3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMYD3, ZMYND1, ZNFN3A1 ([http://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'>[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> | <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> | ||
| - | <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=3mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mek RCSB], [http://www.ebi.ac.uk/pdbsum/3mek PDBsum]</span></td></tr> | + | <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=3mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mek OCA], [http://pdbe.org/3mek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mek RCSB], [http://www.ebi.ac.uk/pdbsum/3mek PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mek ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 17: | Line 20: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3mek ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bochkarev, A]] | [[Category: Bochkarev, A]] | ||
| Line 34: | Line 39: | ||
[[Category: Weigelt, J]] | [[Category: Weigelt, J]] | ||
[[Category: Wu, H]] | [[Category: Wu, H]] | ||
| + | [[Category: Alternative splicing]] | ||
[[Category: Chromatin modification]] | [[Category: Chromatin modification]] | ||
[[Category: Chromatin regulator]] | [[Category: Chromatin regulator]] | ||
| + | [[Category: Cytoplasm]] | ||
[[Category: Di-methylation]] | [[Category: Di-methylation]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
| Line 51: | Line 58: | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Tri-methylation]] | [[Category: Tri-methylation]] | ||
| + | [[Category: Zinc]] | ||
[[Category: Zinc finger mynd domain-containing protein 1]] | [[Category: Zinc finger mynd domain-containing protein 1]] | ||
[[Category: Zinc-finger]] | [[Category: Zinc-finger]] | ||
Current revision
Crystal Structure of Human Histone-Lysine N-methyltransferase SMYD3 in Complex with S-adenosyl-L-methionine
| |||||||||||
Categories: Histone-lysine N-methyltransferase | Human | Arrowsmith, C H | Bochkarev, A | Bountra, C | Dombrovski, L | Edwards, A M | Lam, R | Li, Y | Min, J | Structural genomic | Weigelt, J | Wu, H | Alternative splicing | Chromatin modification | Chromatin regulator | Cytoplasm | Di-methylation | Dna-binding | Histone h3 | Histone methyltransferase | Metal-binding | Methyltransferase | Mynd-type zinc finger | Nucleus | S-adenosyl-l-methionine | Set and mynd domain-containing protein 3 | Set domain | Sgc | Transcriptional activation | Transferase | Tri-methylation | Zinc | Zinc finger mynd domain-containing protein 1 | Zinc-finger
