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<StructureSection load='5e8f' size='340' side='right'caption='[[5e8f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5e8f' size='340' side='right'caption='[[5e8f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e8f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E8F FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e8f]] 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=5E8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8F FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene></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]] 2.1&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene>, <scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE6D, PDED ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PDE6C, PDEA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8f OCA], [https://pdbe.org/5e8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8f RCSB], [https://www.ebi.ac.uk/pdbsum/5e8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8f ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-GMP_phosphodiesterase 3',5'-cyclic-GMP phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.35 3.1.4.35] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8f OCA], [http://pdbe.org/5e8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e8f RCSB], [http://www.ebi.ac.uk/pdbsum/5e8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8f ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/PDE6C_HUMAN PDE6C_HUMAN]] Progressive cone dystrophy;Achromatopsia. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PDE6D_HUMAN PDE6D_HUMAN]] Acts as a GTP specific dissociation inhibitor (GDI). Increases the affinity of ARL3 for GTP by several orders of magnitude and does so by decreasing the nucleotide dissociation rate. Stabilizes Arl3-GTP by decreasing the nucleotide dissociation (By similarity).  
[https://www.uniprot.org/uniprot/PDE6D_HUMAN PDE6D_HUMAN] Acts as a GTP specific dissociation inhibitor (GDI). Increases the affinity of ARL3 for GTP by several orders of magnitude and does so by decreasing the nucleotide dissociation rate. Stabilizes Arl3-GTP by decreasing the nucleotide dissociation (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
This study shows that the prenylated C-terminus of RPGR can bind to PDE6delta with high affinity, suggesting two distinct binding sites of the RPGR/PDE6delta complex. The serine residue at the -3 position relative to the prenylated cysteine seems to play a key role in defining the selectivity of PDE6delta towards ciliary prenylated cargo. [Image: see text]
 
The N- and C-terminal ends of RPGR can bind to PDE6delta.,Fansa EK, O'Reilly NJ, Ismail S, Wittinghofer A EMBO Rep. 2015 Dec;16(12):1583-5. doi: 10.15252/embr.201541404. Epub 2015 Nov 9. PMID:26553937<ref>PMID:26553937</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e8f" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 3',5'-cyclic-GMP phosphodiesterase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fansa, E K]]
[[Category: Fansa EK]]
[[Category: Ismail, S A]]
[[Category: Ismail SA]]
[[Category: Reilly, N J.O]]
[[Category: O'Reilly NJ]]
[[Category: Wittinghofer, A]]
[[Category: Wittinghofer A]]
[[Category: Geranylgeranyl]]
[[Category: Hydrolase]]
[[Category: Immunoglobulin-like beta sandwitch fold]]
[[Category: Prenyl binding protein]]
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