5sih
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of human phosphodiesterase 10 in complex with 6-(3-methylphenyl)sulfanyl-2-(4-pyridin-2-ylpiperazin-1-yl)-9H-purine== | |
| - | + | <StructureSection load='5sih' size='340' side='right'caption='[[5sih]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5sih]] is a 4 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=5SIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SIH 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]] 1.9Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=JPF:6-[(3-methylphenyl)sulfanyl]-2-[4-(pyridin-2-yl)piperazin-1-yl]-9H-purine'>JPF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[https://proteopedia.org/fgij/fg.htm?mol=5sih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sih OCA], [https://pdbe.org/5sih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sih RCSB], [https://www.ebi.ac.uk/pdbsum/5sih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sih ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PDE10_HUMAN PDE10_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.<ref>PMID:17389385</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Benz J]] | ||
| + | [[Category: Brunner M]] | ||
| + | [[Category: Flohr A]] | ||
| + | [[Category: Joseph C]] | ||
| + | [[Category: Rudolph MG]] | ||
Revision as of 07:00, 3 April 2024
Crystal Structure of human phosphodiesterase 10 in complex with 6-(3-methylphenyl)sulfanyl-2-(4-pyridin-2-ylpiperazin-1-yl)-9H-purine
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Categories: Homo sapiens | Large Structures | Benz J | Brunner M | Flohr A | Joseph C | Rudolph MG
