5sg9: Difference between revisions

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==Crystal Structure of human phosphodiesterase 10 in complex with 2-[(E)-2-(4-methyl-6-pyrrolidin-1-ylpyrimidin-2-yl)ethenyl]quinoline==
==CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 10 IN COMPLEX WITH c1(cc(nc(n1)\\C=C\\c3nc2ccccc2cc3)C)N4CCCC4, micromolar IC50=0.536555==
<StructureSection load='5sg9' size='340' side='right'caption='[[5sg9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
<StructureSection load='5sg9' size='340' side='right'caption='[[5sg9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5sg9]] 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=5SG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SG9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5sg9]] 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=5SG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SG9 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]] 2.13&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13&#8491;</td></tr>
<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=IWC:2-{(E)-2-[4-methyl-6-(pyrrolidin-1-yl)pyrimidin-2-yl]ethenyl}quinoline'>IWC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<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=IWC:2-[(~{E})-2-(4-methyl-6-pyrrolidin-1-yl-pyrimidin-2-yl)ethenyl]quinoline'>IWC</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=5sg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sg9 OCA], [https://pdbe.org/5sg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sg9 RCSB], [https://www.ebi.ac.uk/pdbsum/5sg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sg9 ProSAT]</span></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=5sg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sg9 OCA], [https://pdbe.org/5sg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sg9 RCSB], [https://www.ebi.ac.uk/pdbsum/5sg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sg9 ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 10:32, 17 October 2024

CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 10 IN COMPLEX WITH c1(cc(nc(n1)\\C=C\\c3nc2ccccc2cc3)C)N4CCCC4, micromolar IC50=0.536555CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 10 IN COMPLEX WITH c1(cc(nc(n1)\\C=C\\c3nc2ccccc2cc3)C)N4CCCC4, micromolar IC50=0.536555

Structural highlights

5sg9 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.13Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

References

  1. Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H. Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. PMID:17389385

5sg9, resolution 2.13Å

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