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.
4h12
From Proteopedia
| Line 1: | Line 1: | ||
| + | |||
==The crystal structure of methyltransferase domain of human SET domain-containing protein 2 in complex with S-adenosyl-L-homocysteine== | ==The crystal structure of methyltransferase domain of human SET domain-containing protein 2 in complex with S-adenosyl-L-homocysteine== | ||
<StructureSection load='4h12' size='340' side='right' caption='[[4h12]], [[Resolution|resolution]] 2.06Å' scene=''> | <StructureSection load='4h12' size='340' side='right' caption='[[4h12]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4h12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4h12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h6l 3h6l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H12 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069 ([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">SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069 ([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=4h12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h12 RCSB], [http://www.ebi.ac.uk/pdbsum/4h12 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=4h12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h12 OCA], [http://pdbe.org/4h12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h12 RCSB], [http://www.ebi.ac.uk/pdbsum/4h12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h12 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4h12" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 26: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Amaya, M F]] | [[Category: Amaya, M F]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 23:21, 4 August 2016
The crystal structure of methyltransferase domain of human SET domain-containing protein 2 in complex with S-adenosyl-L-homocysteine
| |||||||||||
Categories: Histone-lysine N-methyltransferase | Human | Amaya, M F | Arrowsmith, C H | Bountra, C | Bunnage, M | Dong, A | Edwards, A M | Mackenzie, F | Min, J | Structural genomic | Weigelt, J | Wu, H | Zeng, H | Activator | Chromatin regulator | Dna-binding | Methylation | Methyltransferase | Nucleus | Phosphoprotein | S-adenosyl-l-homocysteine | Set domain-containing protein 2 | Sgc | Transcription | Transcription regulation | Transferase
