2bug: Difference between revisions

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-==SOLUTION STRUCTURE OF THE TPR DOMAIN FROM PROTEIN PHOSPHATASE 5 IN COMPLEX WITH HSP90 DERIVED PEPTIDE==
-<StructureSection load='2bug' size='340' side='right' caption='[[2bug]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
+==Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide==
+<StructureSection load='2bug' size='340' side='right'caption='[[2bug]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUG FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a17|1a17]], [[1s95|1s95]], [[1wao|1wao]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=2bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bug OCA], [https://pdbe.org/2bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bug RCSB], [https://www.ebi.ac.uk/pdbsum/2bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bug ProSAT]</span></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=2bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bug OCA], [http://pdbe.org/2bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bug RCSB], [http://www.ebi.ac.uk/pdbsum/2bug PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PPP5_HUMAN PPP5_HUMAN] May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bug_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bug_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bug ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 31: @@
 ==See Also==
-*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
+*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Barford, D]]
+[[Category: Barford D]]
-[[Category: Cliff, M J]]
+[[Category: Cliff MJ]]
-[[Category: Harris, R]]
+[[Category: Harris R]]
-[[Category: Ladbury, J E]]
+[[Category: Ladbury JE]]
-[[Category: Williams, M A]]
+[[Category: Williams MA]]
-[[Category: Hsp90 binding]]
-[[Category: Hydrolase]]
-[[Category: Iron]]
-[[Category: Manganese]]
-[[Category: Metal-binding]]
-[[Category: Protein phosphatase]]
-[[Category: Tetratricopeptide domain]]