5fzo: Difference between revisions
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<StructureSection load='5fzo' size='340' side='right'caption='[[5fzo]], [[Resolution|resolution]] 1.84Å' scene=''> | <StructureSection load='5fzo' size='340' side='right'caption='[[5fzo]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fzo]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5fzo]] is a 2 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=5FZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FZO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=5fzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzo OCA], [https://pdbe.org/5fzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fzo RCSB], [https://www.ebi.ac.uk/pdbsum/5fzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzo ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/JHD2C_HUMAN JHD2C_HUMAN] Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). | ||
==See Also== | |||
*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fairhead | [[Category: Fairhead M]] | ||
[[Category: Goubin | [[Category: Goubin S]] | ||
[[Category: Johansson | [[Category: Johansson C]] | ||
[[Category: Krojer | [[Category: Krojer T]] | ||
[[Category: McDonough | [[Category: McDonough M]] | ||
[[Category: Nowak | [[Category: Nowak R]] | ||
[[Category: Oppermann | [[Category: Oppermann U]] | ||
[[Category: Talon | [[Category: Talon R]] | ||
Latest revision as of 16:33, 26 July 2023
Crystal structure of the catalytic domain of human JmjD1CCrystal structure of the catalytic domain of human JmjD1C
Structural highlights
FunctionJHD2C_HUMAN Probable histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May be involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes (By similarity). See Also |
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