5si4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of human phosphodiesterase 10 in complex with 3-(2-naphthalen-1-ylpyrazol-3-yl)-1-[3-(trifluoromethoxy)phenyl]pyridazin-4-one== | |
| - | + | <StructureSection load='5si4' size='340' side='right'caption='[[5si4]], [[Resolution|resolution]] 2.39Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5si4]] 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=5SI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SI4 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]] 2.39Å</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=JLR:3-[1-(naphthalen-1-yl)-1H-pyrazol-5-yl]-1-[3-(trifluoromethoxy)phenyl]pyridazin-4(1H)-one'>JLR</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=5si4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5si4 OCA], [https://pdbe.org/5si4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5si4 RCSB], [https://www.ebi.ac.uk/pdbsum/5si4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5si4 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: Flohr A]] | ||
| + | [[Category: Joseph C]] | ||
| + | [[Category: Rogers-Evans M]] | ||
| + | [[Category: Rudolph MG]] | ||
Revision as of 07:00, 3 April 2024
Crystal Structure of human phosphodiesterase 10 in complex with 3-(2-naphthalen-1-ylpyrazol-3-yl)-1-[3-(trifluoromethoxy)phenyl]pyridazin-4-one
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