5up0

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==Crystal structure of human PDE1B catalytic domain in complex with inhibitor 3 (6-(4-chlorobenzyl)-8,9,10,11-tetrahydrobenzo[4,5]thieno[3,2-e][1,2,4]triazolo[1,5-c]pyrimidin-5(6H)-one)==
==Crystal structure of human PDE1B catalytic domain in complex with inhibitor 3 (6-(4-chlorobenzyl)-8,9,10,11-tetrahydrobenzo[4,5]thieno[3,2-e][1,2,4]triazolo[1,5-c]pyrimidin-5(6H)-one)==
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<StructureSection load='5up0' size='340' side='right' caption='[[5up0]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
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<StructureSection load='5up0' size='340' side='right'caption='[[5up0]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5up0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UP0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5up0]] is a 1 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=5UP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UP0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8HP:6-[(4-CHLOROPHENYL)METHYL]-8,9,10,11-TETRAHYDRO[1]BENZOTHIENO[3,2-E][1,2,4]TRIAZOLO[1,5-C]PYRIMIDIN-5(6H)-ONE'>8HP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uoy|5uoy]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8HP:6-[(4-CHLOROPHENYL)METHYL]-8,9,10,11-TETRAHYDRO[1]BENZOTHIENO[3,2-E][1,2,4]TRIAZOLO[1,5-C]PYRIMIDIN-5(6H)-ONE'>8HP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5up0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5up0 OCA], [https://pdbe.org/5up0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5up0 RCSB], [https://www.ebi.ac.uk/pdbsum/5up0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5up0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5up0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5up0 OCA], [http://pdbe.org/5up0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5up0 RCSB], [http://www.ebi.ac.uk/pdbsum/5up0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5up0 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PDE1B_HUMAN PDE1B_HUMAN]] Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.
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[https://www.uniprot.org/uniprot/PDE1B_HUMAN PDE1B_HUMAN] Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5up0" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5up0" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
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[[Category: Homo sapiens]]
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[[Category: Aertgeerts, K]]
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[[Category: Large Structures]]
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[[Category: Allerston, C K]]
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[[Category: Aertgeerts K]]
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[[Category: Barker, R]]
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[[Category: Allerston CK]]
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[[Category: Cedervall, E P]]
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[[Category: Barker R]]
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[[Category: Sridhar, V]]
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[[Category: Cedervall EP]]
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[[Category: Xu, R]]
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[[Category: Sridhar V]]
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[[Category: Hydrolase]]
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[[Category: Xu R]]
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[[Category: Hydrolase inhibitor]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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Current revision

Crystal structure of human PDE1B catalytic domain in complex with inhibitor 3 (6-(4-chlorobenzyl)-8,9,10,11-tetrahydrobenzo[4,5]thieno[3,2-e][1,2,4]triazolo[1,5-c]pyrimidin-5(6H)-one)

PDB ID 5up0

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