View source for 5axq


==Crystal structure of the catalytic domain of PDE10A complexed with highly potent and brain-penetrant PDE10A Inhibitor with 2-oxindole scaffold==
<StructureSection load='5axq' size='340' side='right'caption='[[5axq]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5axq]] 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=5AXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AXQ 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]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4LK:3-[3-FLUORANYL-4-[5-METHOXY-4-OXIDANYLIDENE-3-(2-PHENYLPYRAZOL-3-YL)PYRIDAZIN-1-YL]PHENYL]-1,3-OXAZOLIDIN-2-ONE'>4LK</scene>, <scene name='pdbligand=4LP:1-(CYCLOPROPYLMETHYL)-4-FLUORANYL-5-[5-METHOXY-4-OXIDANYLIDENE-3-(2-PHENYLPYRAZOL-3-YL)PYRIDAZIN-1-YL]-3,3-DIMETHYL-INDOL-2-ONE'>4LP</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=5axq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5axq OCA], [https://pdbe.org/5axq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5axq RCSB], [https://www.ebi.ac.uk/pdbsum/5axq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5axq 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> 

==See Also==
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oki H]]
[[Category: Zama Y]]