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2w5y
From Proteopedia
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<StructureSection load='2w5y' size='340' side='right'caption='[[2w5y]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2w5y' size='340' side='right'caption='[[2w5y]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2w5y]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2w5y]] 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=2W5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W5Y FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2agh|2agh]], [[2j2s|2j2s]], [[2w5z|2w5z]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2agh|2agh]], [[2j2s|2j2s]], [[2w5z|2w5z]]</div></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=2w5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w5y OCA], [https://pdbe.org/2w5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w5y RCSB], [https://www.ebi.ac.uk/pdbsum/2w5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w5y ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 10:58, 6 April 2022
Binary Complex of the Mixed Lineage Leukaemia (MLL1) SET Domain with the cofactor product S-Adenosylhomocysteine.
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Odho, Z | Roe, S M | Southall, S M | WIlson, J R | Wong, P S | Alternative splicing | Apoptosis | Bromodomain | Chromatin regulator | Chromosomal rearrangement | Dna-binding | Histone modification | Kmt2a | Metal-binding | Methyltransferase | Mixed lineage leukaemia | Mll1 | Nucleus | Phosphoprotein | Polymorphism | Protein lysine methyltransferase | Proto-oncogene | S-adenosyl-l-methionine | Set domain | Transcription | Transcription regulation | Transferase | Ubl conjugation | Zinc | Zinc-finger

