4bbq
From Proteopedia
(Difference between revisions)
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<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution|resolution]] 2.24Å' scene=''> | <StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4bbq]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4bbq]] is a 2 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBQ 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='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_H3]-lysine-36_demethylase [Histone H3]-lysine-36 demethylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.27 1.14.11.27] </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=4bbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbq OCA], [https://pdbe.org/4bbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbq RCSB], [https://www.ebi.ac.uk/pdbsum/4bbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbq ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/KDM2A_HUMAN KDM2A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.<ref>PMID:16362057</ref> <ref>PMID:19001877</ref> |
==See Also== | ==See Also== | ||
Revision as of 07:07, 31 August 2022
Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)
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Categories: Human | Large Structures | Allerston, C K | Arrowsmith, C H | Ball, L | Bountra, C | Chen, Y | Delft, F von | Edlich, C | Edwards, A | Gileadi, O | Krojer, T | Laue, E D | Li, B | Watson, A A | Chromatin | Cpg island | Demethylation | Fbxl11 | Kdm2a | Ligase | Oxidoreductase | Ubiquitin | Ubiquitination | Zf-cxxc dna binding domain
