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3a1b

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Current revision (14:06, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3a1b' size='340' side='right'caption='[[3a1b]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='3a1b' size='340' side='right'caption='[[3a1b]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[3a1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.292&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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>
<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>
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== Function ==
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[https://www.uniprot.org/uniprot/DNM3A_HUMAN DNM3A_HUMAN] Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZNF238. Can actively repress transcription through the recruitment of HDAC activity (By similarity).<ref>PMID:16357870</ref> [https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arita, K]]
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[[Category: Arita K]]
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[[Category: Ariyoshi, M]]
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[[Category: Ariyoshi M]]
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[[Category: Otani, J]]
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[[Category: Otani J]]
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[[Category: Shirakawa, M]]
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[[Category: Shirakawa M]]
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[[Category: Alternative promoter usage]]
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[[Category: Chromosomal protein]]
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[[Category: Dna damage]]
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[[Category: Dna repair]]
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[[Category: Dna-binding]]
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[[Category: Histone binding]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Methyltransferase]]
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[[Category: Nucleosome core]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Transferase]]
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[[Category: Zinc-finger]]
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Current revision

Crystal structure of the DNMT3A ADD domain in complex with histone H3

PDB ID 3a1b

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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