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- PDB-4e17: Alpha-E-catenin is an autoinhibited molecule that co-activates vi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4.0E+17 | ||||||
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Title | Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin | ||||||
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![]() | CELL ADHESION / four helix bundle | ||||||
Function / homology | ![]() muscle tendon junction / negative regulation of integrin-mediated signaling pathway / Platelet degranulation / Smooth Muscle Contraction / VEGFR2 mediated vascular permeability / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web ...muscle tendon junction / negative regulation of integrin-mediated signaling pathway / Platelet degranulation / Smooth Muscle Contraction / VEGFR2 mediated vascular permeability / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / RHO GTPases activate IQGAPs / Adherens junctions interactions / gamma-catenin binding / epithelial cell-cell adhesion / zonula adherens / gap junction assembly / dystroglycan binding / cellular response to indole-3-methanol / muscle alpha-actinin binding / MAP2K and MAPK activation / alpha-catenin binding / vinculin binding / flotillin complex / fascia adherens / negative regulation of cell motility / cell-cell contact zone / Myogenesis / adherens junction assembly / apical junction assembly / costamere / regulation of establishment of endothelial barrier / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of smoothened signaling pathway / catenin complex / axon extension / protein localization to cell surface / negative regulation of protein localization to nucleus / axon regeneration / lamellipodium assembly / regulation of focal adhesion assembly / negative regulation of neuroblast proliferation / smoothened signaling pathway / establishment or maintenance of cell polarity / alpha-actinin binding / odontogenesis of dentin-containing tooth / brush border / skeletal muscle myofibril / intercalated disc / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / neuroblast proliferation / stress fiber / ovarian follicle development / extrinsic apoptotic signaling pathway in absence of ligand / regulation of cell migration / acrosomal vesicle / Neutrophil degranulation / cell projection / integrin-mediated signaling pathway / morphogenesis of an epithelium / cell motility / adherens junction / neuromuscular junction / protein localization / sarcolemma / beta-catenin binding / Z disc / cell-cell adhesion / response to estrogen / male gonad development / cell-cell junction / actin filament binding / cell migration / actin cytoskeleton / lamellipodium / regulation of cell population proliferation / scaffold protein binding / mitochondrial inner membrane / cytoskeleton / cell adhesion / cadherin binding / focal adhesion / apoptotic process / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / structural molecule activity / protein homodimerization activity / protein-containing complex / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Choi, H.-J. / Pokutta, S. / Cadwell, G.W. / Bankston, L.A. / Liddington, R.C. / Weis, W.I. | ||||||
![]() | ![]() Title: Conformational plasticity of alpha-catenin revealed by binding interactions with vinculin Authors: Choi, H.-J. / Pokutta, S. / Bankston, L. / Liddington, R. / Weis, W.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.7 KB | Display | ![]() |
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PDB format | ![]() | 93.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.4 KB | Display | ![]() |
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Full document | ![]() | 440 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 15.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4e18C ![]() 1t01S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29379.932 Da / Num. of mol.: 1 / Fragment: D1 domain (UNP residues 1-259) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 4403.830 Da / Num. of mol.: 1 / Fragment: vinculin binding domain (UNP residues 321-356) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.29 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 20% PEG8000, 100 mM MES, pH 6.8, 3 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 283K |
-Data collection
Diffraction | Mean temperature: 193 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 7, 2011 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.3→50 Å / Num. obs: 16376 / % possible obs: 97.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.5 % / Rmerge(I) obs: 0.078 / Χ2: 1.684 / Net I/σ(I): 11.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1T01 Resolution: 2.304→42.133 Å / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.8356 / SU ML: 0.25 / σ(F): 1.34 / Phase error: 22.95 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 1.11 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 47.345 Å2 / ksol: 0.375 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 149.53 Å2 / Biso mean: 50.4 Å2 / Biso min: 18.16 Å2
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Refinement step | Cycle: LAST / Resolution: 2.304→42.133 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 9
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Refinement TLS params. | S33: 0 Å ° / Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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