1so2: Difference between revisions

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<StructureSection load='1so2' size='340' side='right'caption='[[1so2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1so2' size='340' side='right'caption='[[1so2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1so2]] 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=1SO2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SO2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1so2]] 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=1SO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SO2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=666:6-(4-{[2-(3-IODOBENZYL)-3-OXOCYCLOHEX-1-EN-1-YL]AMINO}PHENYL)-5-METHYL-4,5-DIHYDROPYRIDAZIN-3(2H)-ONE'>666</scene>, <scene name='pdbligand=HG9:1-DEOXY-1-[(2-HYDROXYETHYL)(NONANOYL)AMINO]HEXITOL'>HG9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1soj|1soj]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=666:6-(4-{[2-(3-IODOBENZYL)-3-OXOCYCLOHEX-1-EN-1-YL]AMINO}PHENYL)-5-METHYL-4,5-DIHYDROPYRIDAZIN-3(2H)-ONE'>666</scene>, <scene name='pdbligand=HG9:1-DEOXY-1-[(2-HYDROXYETHYL)(NONANOYL)AMINO]HEXITOL'>HG9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE3B ([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=1so2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1so2 OCA], [https://pdbe.org/1so2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1so2 RCSB], [https://www.ebi.ac.uk/pdbsum/1so2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1so2 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-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=1so2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1so2 OCA], [http://pdbe.org/1so2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1so2 RCSB], [http://www.ebi.ac.uk/pdbsum/1so2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1so2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PDE3B_HUMAN PDE3B_HUMAN]] Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.<ref>PMID:21393242</ref> <ref>PMID:15147193</ref>
[https://www.uniprot.org/uniprot/PDE3B_HUMAN PDE3B_HUMAN] Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis.<ref>PMID:21393242</ref> <ref>PMID:15147193</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Becker, J W]]
[[Category: Becker JW]]
[[Category: Chung, C]]
[[Category: Chung C]]
[[Category: Edmondson, S D]]
[[Category: Edmondson SD]]
[[Category: Mastracchio, A]]
[[Category: Mastracchio A]]
[[Category: Parmee, E R]]
[[Category: Parmee ER]]
[[Category: Patel, S B]]
[[Category: Patel SB]]
[[Category: Ploeg, L H.Van Der]]
[[Category: Scapin G]]
[[Category: Scapin, G]]
[[Category: Singh SB]]
[[Category: Singh, S B]]
[[Category: Tota MR]]
[[Category: Tota, M R]]
[[Category: Van Der Ploeg LH]]
[[Category: Varnerin, J P]]
[[Category: Varnerin JP]]
[[Category: Hydrolase]]
[[Category: Pde3b phosphodiesterase]]
Retrieved from "https://proteopedia.org/1so2"