4bbq

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Current revision (10:59, 9 May 2024) (edit) (undo)
 
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<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
<StructureSection load='4bbq' size='340' side='right'caption='[[4bbq]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[4bbq]] 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=4BBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBQ 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]] 2.24&#8491;</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/[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>
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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>
<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>
<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 ==
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[[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>
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[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==
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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: Allerston, C K]]
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[[Category: Allerston CK]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Ball, L]]
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[[Category: Ball L]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Chen, Y]]
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[[Category: Chen Y]]
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[[Category: Delft, F von]]
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[[Category: Edlich C]]
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[[Category: Edlich, C]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: Gileadi O]]
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[[Category: Gileadi, O]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Laue ED]]
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[[Category: Laue, E D]]
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[[Category: Li B]]
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[[Category: Li, B]]
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[[Category: Watson AA]]
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[[Category: Watson, A A]]
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[[Category: Von Delft F]]
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[[Category: Chromatin]]
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[[Category: Cpg island]]
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[[Category: Demethylation]]
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[[Category: Fbxl11]]
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[[Category: Kdm2a]]
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[[Category: Ligase]]
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[[Category: Oxidoreductase]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitination]]
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[[Category: Zf-cxxc dna binding domain]]
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Current revision

Crystal structure of the CXXC and PHD domain of Human Lysine-specific Demethylase 2A (KDM2A)(FBXL11)

PDB ID 4bbq

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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