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Open data
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Basic information
Entry | Database: PDB / ID: 2oun | ||||||
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Title | crystal structure of PDE10A2 in complex with AMP | ||||||
![]() | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A | ||||||
![]() | HYDROLASE / pde / product binding | ||||||
Function / homology | ![]() cGMP-stimulated cyclic-nucleotide phosphodiesterase activity / 3',5'-cyclic-nucleotide phosphodiesterase / negative regulation of cGMP-mediated signaling / cGMP catabolic process / cGMP effects / cAMP catabolic process / 3',5'-cyclic-nucleotide phosphodiesterase activity / cGMP binding / 3',5'-cyclic-GMP phosphodiesterase activity / 3',5'-cyclic-AMP phosphodiesterase activity ...cGMP-stimulated cyclic-nucleotide phosphodiesterase activity / 3',5'-cyclic-nucleotide phosphodiesterase / negative regulation of cGMP-mediated signaling / cGMP catabolic process / cGMP effects / cAMP catabolic process / 3',5'-cyclic-nucleotide phosphodiesterase activity / cGMP binding / 3',5'-cyclic-GMP phosphodiesterase activity / 3',5'-cyclic-AMP phosphodiesterase activity / cAMP binding / cAMP-mediated signaling / G alpha (s) signalling events / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wang, H.C. / Liu, Y.D. / Hou, J. / Zheng, M.Y. / Robinson, H. / Ke, H.M. | ||||||
![]() | ![]() Title: From the Cover: Structural insight into substrate specificity of phosphodiesterase 10. Authors: Wang, H. / Liu, Y. / Hou, J. / Zheng, M. / Robinson, H. / Ke, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 150.6 KB | Display | ![]() |
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PDB format | ![]() | 117.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 760.3 KB | Display | ![]() |
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Full document | ![]() | 770.5 KB | Display | |
Data in XML | ![]() | 28.7 KB | Display | |
Data in CIF | ![]() | 41.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2oupC ![]() 2ouqC ![]() 2ourC ![]() 2ousC ![]() 2ouuC ![]() 2ouvC ![]() 2ouyC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | two molecules in the crystallographic asymmetric unit may not be biologically relevant. |
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Components
#1: Protein | Mass: 38306.078 Da / Num. of mol.: 2 / Fragment: catalytic domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9Y233, 3',5'-cyclic-nucleotide phosphodiesterase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-AMP / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.98 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: The native PDE10A2 crystals were grown against a well buffer of 0.1 M HEPES (pH 7.5), 0.2 M MgCl2, 50 mM beta-mercaptoethanol(BME), and 16% PEG3350. The complex of PDE10A2-AMP was prepared ...Details: The native PDE10A2 crystals were grown against a well buffer of 0.1 M HEPES (pH 7.5), 0.2 M MgCl2, 50 mM beta-mercaptoethanol(BME), and 16% PEG3350. The complex of PDE10A2-AMP was prepared by soaking the crystals in 20 mM cAMP, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 15, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.56→30 Å / Num. obs: 87893 / % possible obs: 93.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.2 % / Rmerge(I) obs: 0.094 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDE10A2 native Resolution: 1.56→30 Å / Isotropic thermal model: isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 19.5 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.56→30 Å
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Refine LS restraints |
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