3a1b
From Proteopedia
(Difference between revisions)
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<StructureSection load='3a1b' size='340' side='right'caption='[[3a1b]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='3a1b' size='340' side='right'caption='[[3a1b]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a1b]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3a1b]] 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=3A1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A1B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=EDO:1,2-ETHANEDIOL'>EDO</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">[[3a1a|3a1a]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a1a|3a1a]]</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/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </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=3a1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a1b OCA], [https://pdbe.org/3a1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a1b RCSB], [https://www.ebi.ac.uk/pdbsum/3a1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a1b ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 16:14, 22 December 2021
Crystal structure of the DNMT3A ADD domain in complex with histone H3
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Categories: Human | Large Structures | Arita, K | Ariyoshi, M | Otani, J | Shirakawa, M | Alternative promoter usage | Chromosomal protein | Dna damage | Dna repair | Dna-binding | Histone binding | Metal-binding | Methylation | Methyltransferase | Nucleosome core | Nucleus | Phosphoprotein | S-adenosyl-l-methionine | Transferase | Zinc-finger

