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Open data
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Basic information
Entry | Database: PDB / ID: 2ouy | ||||||
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Title | crystal structure of pde10a2 mutant D564A in complex with cAMP. | ||||||
![]() | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A | ||||||
![]() | HYDROLASE / pde / substrate specificity / cAMP | ||||||
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. | ||||||
![]() | ![]() 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 | ![]() | 146.4 KB | Display | ![]() |
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PDB format | ![]() | 114.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 750.6 KB | Display | ![]() |
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Full document | ![]() | 762.7 KB | Display | |
Data in XML | ![]() | 28.2 KB | Display | |
Data in CIF | ![]() | 40.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ounC ![]() 2oupC ![]() 2ouqC ![]() 2ourC ![]() 2ousC ![]() 2ouuC ![]() 2ouvC 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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2 | ![]()
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Unit cell |
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Details | Two moleucles in the asymmetric unit are not related by 2-fold axid. |
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Components
#1: Protein | Mass: 38305.094 Da / Num. of mol.: 2 / Fragment: catalytic domain / Mutation: D564N 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-CMP / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.49 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: D564N and D674A mutants were crystallized against a well buffer of 0.1 M HEPES, pH 7.5, 0.1 M MgCl2, 100 mM BME, and 13% PEG3350. The D564N crystals were soaked in 20 mM cAMP in a buffer of ...Details: D564N and D674A mutants were crystallized against a well buffer of 0.1 M HEPES, pH 7.5, 0.1 M MgCl2, 100 mM BME, and 13% PEG3350. The D564N crystals were soaked in 20 mM cAMP in a buffer of 16% PEG8000, 0.1 M HEPES, pH 7.5, 0.1 M MgCl2, 60 mM BME for 1.5 hours, 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: Apr 27, 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: 1.9→30 Å / Num. obs: 47078 / % possible obs: 92.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 7.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pde10a2 native Resolution: 1.9→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: 26.9 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
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Refine LS restraints |
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