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6a58

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<StructureSection load='6a58' size='340' side='right'caption='[[6a58]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
<StructureSection load='6a58' size='340' side='right'caption='[[6a58]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6a58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A58 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6a58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A58 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.57&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6a57|6a57]]</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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=6a58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a58 OCA], [http://pdbe.org/6a58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a58 RCSB], [http://www.ebi.ac.uk/pdbsum/6a58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a58 ProSAT]</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=6a58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a58 OCA], [https://pdbe.org/6a58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a58 RCSB], [https://www.ebi.ac.uk/pdbsum/6a58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a58 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/REF6_ARATH REF6_ARATH]] Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3. Demethylates both tri- (H3K27me3) and di-methylated (H3K27me2) H3K27me (PubMed:21642989, PubMed:27111035). Demethylates also H3K4me3/2 and H3K36me3/2 in an in vitro assay (PubMed:20711170). Involved in the transcriptional regulation of hundreds of genes regulating developmental patterning and responses to various stimuli (PubMed:18467490). Binds DNA via its four zinc fingers in a sequence-specific manner, 5'-CTCTGYTY-3', to promote the demethylation of H3K27me3 and the regulation of organ boundary formation (PubMed:27111034, PubMed:27111035). Involved in the regulation of flowering time by repressing FLOWERING LOCUS C (FLC) expression (PubMed:15377760). Interacts with the NF-Y complexe to regulate SOC1 (PubMed:25105952). Mediates the recruitment of BRM to its target loci (PubMed:27111034).<ref>PMID:15377760</ref> <ref>PMID:18467490</ref> <ref>PMID:20711170</ref> <ref>PMID:21642989</ref> <ref>PMID:25105952</ref> <ref>PMID:27111034</ref> <ref>PMID:27111035</ref>
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[https://www.uniprot.org/uniprot/REF6_ARATH REF6_ARATH] Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3. Demethylates both tri- (H3K27me3) and di-methylated (H3K27me2) H3K27me (PubMed:21642989, PubMed:27111035). Demethylates also H3K4me3/2 and H3K36me3/2 in an in vitro assay (PubMed:20711170). Involved in the transcriptional regulation of hundreds of genes regulating developmental patterning and responses to various stimuli (PubMed:18467490). Binds DNA via its four zinc fingers in a sequence-specific manner, 5'-CTCTGYTY-3', to promote the demethylation of H3K27me3 and the regulation of organ boundary formation (PubMed:27111034, PubMed:27111035). Involved in the regulation of flowering time by repressing FLOWERING LOCUS C (FLC) expression (PubMed:15377760). Interacts with the NF-Y complexe to regulate SOC1 (PubMed:25105952). Mediates the recruitment of BRM to its target loci (PubMed:27111034).<ref>PMID:15377760</ref> <ref>PMID:18467490</ref> <ref>PMID:20711170</ref> <ref>PMID:21642989</ref> <ref>PMID:25105952</ref> <ref>PMID:27111034</ref> <ref>PMID:27111035</ref>
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==See Also==
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*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Z]]
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[[Category: Chen Z]]
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[[Category: Tian, Z]]
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[[Category: Tian Z]]
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[[Category: Complex]]
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[[Category: Dna]]
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[[Category: Dna binding protein]]
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[[Category: Histone demethylase ref6]]
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[[Category: Zinc finger]]
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Current revision

Structure of histone demethylase REF6

PDB ID 6a58

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