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5wg8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of PP5C with LB-100; 7-oxabicyclo[2.2.1]heptane-2,3-dicarbonyl moiety modeled in the density== | |
| - | + | <StructureSection load='5wg8' size='340' side='right' caption='[[5wg8]], [[Resolution|resolution]] 1.65Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5wg8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WG8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LB1:(1S,2R,3S,4R)-3-(4-methylpiperazine-1-carbonyl)-7-oxabicyclo[2.2.1]heptane-2-carboxylic+acid'>LB1</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | |
| - | [[Category: | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wg8 OCA], [http://pdbe.org/5wg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wg8 RCSB], [http://www.ebi.ac.uk/pdbsum/5wg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wg8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phosphoprotein phosphatase]] | ||
| + | [[Category: Arcy, B M.D]] | ||
| + | [[Category: Honkanen, R E]] | ||
| + | [[Category: Prakash, A]] | ||
| + | [[Category: Swingle, M R]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase inhibitor]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Revision as of 07:27, 18 July 2018
Structure of PP5C with LB-100; 7-oxabicyclo[2.2.1]heptane-2,3-dicarbonyl moiety modeled in the density
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