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5r7x
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5r7x is ON HOLD Authors: Snee, M., Nowak, R., Johansson, C., Burgess-Brown, N.A., Arrowsmith, C.H, Bountra, C., Edwards, A.M, Oppermann, U. Descrip...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==PanDDA analysis group deposition of ground-state model of Human JMJD1B== | |
| + | <StructureSection load='5r7x' size='340' side='right'caption='[[5r7x]], [[Resolution|resolution]] 1.44Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5r7x]] 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=5R7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5R7X 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]] 1.44Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5r7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5r7x OCA], [https://pdbe.org/5r7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5r7x RCSB], [https://www.ebi.ac.uk/pdbsum/5r7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5r7x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KDM3B_HUMAN KDM3B_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity.<ref>PMID:16603237</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Burgess-Brown | + | </StructureSection> |
| - | [[Category: Edwards | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Snee | + | [[Category: Bountra C]] |
| + | [[Category: Burgess-Brown NA]] | ||
| + | [[Category: Edwards AM]] | ||
| + | [[Category: Johansson C]] | ||
| + | [[Category: Nowak R]] | ||
| + | [[Category: Oppermann U]] | ||
| + | [[Category: Snee M]] | ||
Current revision
PanDDA analysis group deposition of ground-state model of Human JMJD1B
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