9phv: Difference between revisions
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==Crystal structure of human KDM2A with substrate competitive inhibitor 183c== | |||
<StructureSection load='9phv' size='340' side='right'caption='[[9phv]], [[Resolution|resolution]] 2.16Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9phv]] 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=9PHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PHV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1CIP:2-[6-[(3~{R},4~{R})-1-cyclobutyl-4-ethyl-piperidin-3-yl]carbonyl-2-methoxy-naphthalen-1-yl]ethanenitrile'>A1CIP</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
[[Category: Mader | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9phv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9phv OCA], [https://pdbe.org/9phv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9phv RCSB], [https://www.ebi.ac.uk/pdbsum/9phv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9phv ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[Category: Sicheri | [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> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mader P]] | |||
[[Category: Mao DYL]] | |||
[[Category: Pau VPT]] | |||
[[Category: Sicheri F]] | |||
Latest revision as of 12:48, 1 July 2026
Crystal structure of human KDM2A with substrate competitive inhibitor 183c
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