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- PDB-3hvq: Crystal structure of a complex between Protein Phosphatase 1 alph... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3hvq | ||||||
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Title | Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of Neurabin | ||||||
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![]() | HYDROLASE/HYDROLASE REGULATOR / PP1 / NEURABIN / SERINE/THREONINE PHOSPHATASE / POST SYNAPTIC DENSITY / GLUTAMETERGIC RECEPTORS / CARBOHYDRATE METABOLISM / CELL CYCLE / CELL DIVISION / GLYCOGEN METABOLISM / HYDROLASE / IRON / MANGANESE / METAL-BINDING / PHOSPHOPROTEIN / PROTEIN PHOSPHATASE / ACTIN-BINDING / CELL JUNCTION / CELL PROJECTION / CYTOSKELETON / DEVELOPMENTAL PROTEIN / DIFFERENTIATION / NEUROGENESIS / NUCLEUS / SYNAPSE / Synaptosome / HYDROLASE-HYDROLASE REGULATOR COMPLEX | ||||||
Function / homology | ![]() growth cone lamellipodium / regulation of synapse structural plasticity / negative regulation of spontaneous neurotransmitter secretion / positive regulation of long-term synaptic depression / regulation of glycogen catabolic process / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / cellular response to toxic substance / postsynaptic actin cytoskeleton organization ...growth cone lamellipodium / regulation of synapse structural plasticity / negative regulation of spontaneous neurotransmitter secretion / positive regulation of long-term synaptic depression / regulation of glycogen catabolic process / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / cellular response to toxic substance / postsynaptic actin cytoskeleton organization / postsynaptic actin cytoskeleton / protein phosphatase 1 binding / cadherin binding involved in cell-cell adhesion / regulation of filopodium assembly / regulation of actin filament polymerization / regulation of dendritic spine morphogenesis / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of canonical Wnt signaling pathway / regulation of translational initiation / negative regulation of stress fiber assembly / regulation of synapse assembly / myosin phosphatase activity / cortical actin cytoskeleton / branching morphogenesis of an epithelial tube / protein serine/threonine phosphatase activity / glycogen metabolic process / positive regulation of dendritic spine development / dendritic spine neck / protein-serine/threonine phosphatase / Triglyceride catabolism / Maturation of hRSV A proteins / entrainment of circadian clock by photoperiod / phosphatase activity / phosphoprotein phosphatase activity / DARPP-32 events / negative regulation of long-term synaptic potentiation / neuron development / ribonucleoprotein complex binding / dephosphorylation / excitatory postsynaptic potential / protein dephosphorylation / Downregulation of TGF-beta receptor signaling / filopodium / calcium-mediated signaling / actin filament organization / adherens junction / response to lead ion / lung development / circadian regulation of gene expression / modulation of chemical synaptic transmission / neuromuscular junction / regulation of circadian rhythm / positive regulation of neuron projection development / neuron projection development / actin filament binding / Circadian Clock / actin cytoskeleton / presynapse / lamellipodium / GTPase binding / growth cone / perikaryon / transmembrane transporter binding / dendritic spine / postsynaptic density / cytoskeleton / cell cycle / protein domain specific binding / cell division / neuronal cell body / glutamatergic synapse / dendrite / protein-containing complex binding / nucleolus / protein kinase binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Critton, D.A. / Ragusa, M.J. / Page, R. / Peti, W. | ||||||
![]() | ![]() Title: Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Authors: Ragusa, M.J. / Dancheck, B. / Critton, D.A. / Nairn, A.C. / Page, R. / Peti, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.5 KB | Display | ![]() |
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PDB format | ![]() | 148.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 476 KB | Display | ![]() |
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Full document | ![]() | 481.8 KB | Display | |
Data in XML | ![]() | 36.6 KB | Display | |
Data in CIF | ![]() | 53.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3eggSC ![]() 3eghC C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Refine code: 5
NCS ensembles :
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Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | Mass: 37349.844 Da / Num. of mol.: 2 / Fragment: CATALYTIC SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P62136, protein-serine/threonine phosphatase #2: Protein | Mass: 18849.867 Da / Num. of mol.: 2 / Fragment: PP1 BINDING AND PDZ DOMAINS Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 4 types, 569 molecules ![](data/chem/img/MN.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-MN / #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.63 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.9 Details: 0.2 M (NH4)2HPO4, 20% PEG 3350, pH 7.9, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Dec 5, 2008 Details: DOUBLE CRYSTAL CHANNEL CUT, SI(111), 1M LONG RH COATED TOROIDAL MIRROR FOR VERTICAL AND HORIZONTAL FOCUSING |
Radiation | Monochromator: SI(111) CHANNEL CUT MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 54834 / Num. obs: 53709 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 25.5 Å2 / Rsym value: 0.103 / Net I/σ(I): 10.4 |
Reflection shell | Resolution: 2.2→2.24 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 5 / Num. unique all: 2731 / Rsym value: 0.263 / % possible all: 97.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3EGG Resolution: 2.2→20 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.926 / SU B: 8.339 / SU ML: 0.113 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.202 / ESU R Free: 0.186 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.592 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.201→2.258 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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