5si7: Difference between revisions

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'''Unreleased structure'''


The entry 5si7 is ON HOLD  until 2024-02-01
==Crystal Structure of human phosphodiesterase 10 in complex with 2-benzyl-6,6-dimethyl-1H-imidazo[4,5-h]isoquinoline-7,9-dione==
 
<StructureSection load='5si7' size='340' side='right'caption='[[5si7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5si7]] 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=5SI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SI7 FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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=JML:2-benzyl-6,6-dimethyl-1H-imidazo[4,5-h]isoquinoline-7,9(6H,8H)-dione'>JML</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=5si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5si7 OCA], [https://pdbe.org/5si7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5si7 RCSB], [https://www.ebi.ac.uk/pdbsum/5si7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5si7 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: Boehringer M]]
[[Category: Flohr A]]
[[Category: Joseph C]]
[[Category: Rudolph MG]]