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4hsu
From Proteopedia
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| - | {{STRUCTURE_4hsu| PDB=4hsu | SCENE= }} | ||
| - | ===Crystal structure of LSD2-NPAC with H3(1-26)in space group P21=== | ||
| - | == | + | ==Crystal structure of LSD2-NPAC with H3(1-26)in space group P21== |
| - | [[http://www. | + | <StructureSection load='4hsu' size='340' side='right'caption='[[4hsu]], [[Resolution|resolution]] 1.99Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hsu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HSU 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]] 1.988Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4hsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hsu OCA], [https://pdbe.org/4hsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hsu RCSB], [https://www.ebi.ac.uk/pdbsum/4hsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hsu 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__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Xenopus laevis]] |
| - | [[Category: | + | [[Category: Chen F]] |
| - | [[Category: | + | [[Category: Dong Z]] |
| - | [[Category: | + | [[Category: Fang J]] |
| - | [[Category: | + | [[Category: Xu Y]] |
Current revision
Crystal structure of LSD2-NPAC with H3(1-26)in space group P21
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Categories: Homo sapiens | Large Structures | Xenopus laevis | Chen F | Dong Z | Fang J | Xu Y
