7xe3: Difference between revisions
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==Crystal structure of LSD2 in complex with compound 7c== | |||
<StructureSection load='7xe3' size='340' side='right'caption='[[7xe3]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xe3]] 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=7XE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XE3 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]] 2.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8A2:3-[4-bromanyl-2,5-bis(fluoranyl)phenyl]propanal'>8A2</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=7xe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xe3 OCA], [https://pdbe.org/7xe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xe3 RCSB], [https://www.ebi.ac.uk/pdbsum/7xe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xe3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KDM1B_HUMAN KDM1B_HUMAN] Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity). | |||
==See Also== | |||
*[[Lysine-specific histone demethylase 3D structures|Lysine-specific histone demethylase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Niwa | [[Category: Homo sapiens]] | ||
[[Category: Sato | [[Category: Large Structures]] | ||
[[Category: Umehara | [[Category: Niwa H]] | ||
[[Category: Sato S]] | |||
[[Category: Umehara T]] |