3ws9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of PDE10A in complex with a benzimdazole inhibitor==
==Crystal structure of PDE10A in complex with a benzimdazole inhibitor==
-
<StructureSection load='3ws9' size='340' side='right' caption='[[3ws9]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
+
<StructureSection load='3ws9' size='340' side='right'caption='[[3ws9]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3ws9]] is a 2 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=3WS9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WS9 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3ws9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WS9 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=X4D:7-[2-(5-METHYL-1-PHENYL-1H-BENZIMIDAZOL-2-YL)ETHYL]IMIDAZO[1,5-B]PYRIDAZINE'>X4D</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=X4D:7-[2-(5-METHYL-1-PHENYL-1H-BENZIMIDAZOL-2-YL)ETHYL]IMIDAZO[1,5-B]PYRIDAZINE'>X4D</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ws8|3ws8]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ws8|3ws8]]</div></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE10A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE10A ([https://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ws9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ws9 OCA], [http://pdbe.org/3ws9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ws9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ws9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ws9 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=3ws9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ws9 OCA], [https://pdbe.org/3ws9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ws9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ws9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ws9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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>
+
[[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 22: Line 22:
==See Also==
==See Also==
-
*[[Phosphodiesterase|Phosphodiesterase]]
+
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 28: Line 28:
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
 +
[[Category: Large Structures]]
[[Category: Amano, Y]]
[[Category: Amano, Y]]
[[Category: Honbou, K]]
[[Category: Honbou, K]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Phosphodiesterase]]
[[Category: Phosphodiesterase]]

Revision as of 05:29, 10 August 2022

Crystal structure of PDE10A in complex with a benzimdazole inhibitor

PDB ID 3ws9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools