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3h63

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==Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)==
==Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)==
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<StructureSection load='3h63' size='340' side='right' caption='[[3h63]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='3h63' size='340' side='right'caption='[[3h63]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3h63]] is a 2 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=3H63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H63 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3h63]] 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=3H63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H63 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NHC:(1R,2S,3R,4S)-2,3-DIMETHYL-7-OXABICYCLO[2.2.1]HEPTANE-2,3-DICARBOXYLIC+ACID'>NHC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h60|3h60]], [[3h61|3h61]], [[3h62|3h62]], [[3h64|3h64]], [[3h66|3h66]], [[3h67|3h67]], [[3h68|3h68]], [[3h69|3h69]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NHC:(1R,2S,3R,4S)-2,3-DIMETHYL-7-OXABICYCLO[2.2.1]HEPTANE-2,3-DICARBOXYLIC+ACID'>NHC</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP5C, PPP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h63 OCA], [https://pdbe.org/3h63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h63 RCSB], [https://www.ebi.ac.uk/pdbsum/3h63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h63 ProSAT]</span></td></tr>
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<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>
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<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=3h63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h63 OCA], [http://pdbe.org/3h63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h63 RCSB], [http://www.ebi.ac.uk/pdbsum/3h63 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h63_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h63_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
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*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
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*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Bertini, I]]
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[[Category: Bertini I]]
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[[Category: Calderone, V]]
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[[Category: Calderone V]]
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[[Category: Fragai, M]]
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[[Category: Fragai M]]
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[[Category: Luchinat, C]]
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[[Category: Luchinat C]]
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[[Category: Talluri, E]]
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[[Category: Talluri E]]
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[[Category: Drug design]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Iron]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Metalloenzyme]]
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[[Category: Nucleus]]
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[[Category: Phosphatase]]
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[[Category: Protein phosphatase]]
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[[Category: Tpr repeat]]
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Current revision

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)

PDB ID 3h63

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