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5pno

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PanDDA analysis group deposition -- Crystal Structure of JMJD2D after initial refinement with no ligand modelled (structure 218)

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 ==PanDDA analysis group deposition -- Crystal Structure of JMJD2D after initial refinement with no ligand modelled (structure 218)==
-<StructureSection load='5pno' size='340' side='right' caption='[[5pno]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='5pno' size='340' side='right'caption='[[5pno]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5pno]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5PNO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5pno]] is a 1 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=5PNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5PNO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KDM4D, JHDM3D, JMJD2D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5pno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5pno OCA], [http://pdbe.org/5pno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5pno RCSB], [http://www.ebi.ac.uk/pdbsum/5pno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5pno 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=5pno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5pno OCA], [https://pdbe.org/5pno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5pno RCSB], [https://www.ebi.ac.uk/pdbsum/5pno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5pno ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
+[https://www.uniprot.org/uniprot/KDM4D_HUMAN KDM4D_HUMAN] Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.<ref>PMID:16603238</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In macromolecular crystallography, the rigorous detection of changed states (for example, ligand binding) is difficult unless signal is strong. Ambiguous ('weak' or 'noisy') density is experimentally common, since molecular states are generally only fractionally present in the crystal. Existing methodologies focus on generating maximally accurate maps whereby minor states become discernible; in practice, such map interpretation is disappointingly subjective, time-consuming and methodologically unsound. Here we report the PanDDA method, which automatically reveals clear electron density for the changed state-even from inaccurate maps-by subtracting a proportion of the confounding 'ground state'; changed states are objectively identified from statistical analysis of density distributions. The method is completely general, implying new best practice for all changed-state studies, including the routine collection of multiple ground-state crystals. More generally, these results demonstrate: the incompleteness of atomic models; that single data sets contain insufficient information to model them fully; and that accuracy requires further map-deconvolution approaches.
-A multi-crystal method for extracting obscured crystallographic states from conventionally uninterpretable electron density.,Pearce NM, Krojer T, Bradley AR, Collins P, Nowak RP, Talon R, Marsden BD, Kelm S, Shi J, Deane CM, von Delft F Nat Commun. 2017 Apr 24;8:15123. doi: 10.1038/ncomms15123. PMID:28436492<ref>PMID:28436492</ref>
+==See Also==
+*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5pno" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H]]
+[[Category: Large Structures]]
-[[Category: Bountra, C]]
+[[Category: Arrowsmith CH]]
-[[Category: Bradley, A R]]
+[[Category: Bountra C]]
-[[Category: Brandao-Neto, J]]
+[[Category: Bradley AR]]
-[[Category: Brennan, P E]]
+[[Category: Brandao-Neto J]]
-[[Category: Burgess-Brown, N]]
+[[Category: Brennan PE]]
-[[Category: Collins, P]]
+[[Category: Burgess-Brown N]]
-[[Category: Cox, O]]
+[[Category: Collins P]]
-[[Category: Delft, F von]]
+[[Category: Cox O]]
-[[Category: Dias, A]]
+[[Category: Dias A]]
-[[Category: Douangamath, A]]
+[[Category: Douangamath A]]
-[[Category: Edwards, A]]
+[[Category: Edwards A]]
-[[Category: Fairhead, M]]
+[[Category: Fairhead M]]
-[[Category: Krojer, T]]
+[[Category: Krojer T]]
-[[Category: MacLean, E]]
+[[Category: MacLean E]]
-[[Category: Ng, J]]
+[[Category: Ng J]]
-[[Category: Oppermann, U]]
+[[Category: Oppermann U]]
-[[Category: Pearce, N M]]
+[[Category: Pearce NM]]
-[[Category: Renjie, Z]]
+[[Category: Renjie Z]]
-[[Category: Sethi, R]]
+[[Category: Sethi R]]
-[[Category: Szykowska, A]]
+[[Category: Szykowska A]]
-[[Category: Talon, R]]
+[[Category: Talon R]]
-[[Category: Vollmar, M]]
+[[Category: Vollmar M]]
-[[Category: Wright, N]]
+[[Category: Wright N]]
-[[Category: Epigenetic]]
+[[Category: Von Delft F]]
-[[Category: Jmj domain]]
-[[Category: Oxidoreductase]]
-[[Category: Pandda]]
-[[Category: Sgc - diamond i04-1 fragment screening]]

5pno

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Current revision

PanDDA analysis group deposition -- Crystal Structure of JMJD2D after initial refinement with no ligand modelled (structure 218)

Structural highlights

Function

See Also

References

Contents

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