5si8: Difference between revisions
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==Crystal Structure of human phosphodiesterase 10 in complex with N-(6-cyano-2-phenylimidazo[1,2-a]pyridin-7-yl)-1-methyl-4-(morpholine-4-carbonyl)pyrazole-3-carboxamide== | |||
<StructureSection load='5si8' size='340' side='right'caption='[[5si8]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5si8]] 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=5SI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SI8 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]] 2.1Å</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=JMU:N-[(4R)-6-cyano-2-phenylimidazo[1,2-a]pyridin-7-yl]-1-methyl-4-(morpholine-4-carbonyl)-1H-pyrazole-3-carboxamide'>JMU</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=5si8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5si8 OCA], [https://pdbe.org/5si8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5si8 RCSB], [https://www.ebi.ac.uk/pdbsum/5si8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5si8 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: Peters J]] | |||
[[Category: Rudolph MG]] | |||