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Open data
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Basic information
Entry | Database: PDB / ID: 5y3b | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Title | Crystal structure of mouse Ccd1 DIX domain | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Dixin | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
![]() | SIGNALING PROTEIN / Wnt signal | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Function / homology | ![]() forebrain ventricular zone progenitor cell division / cerebral cortex radially oriented cell migration / cell proliferation in forebrain / cerebellar cortex development / mitogen-activated protein kinase kinase kinase binding / gamma-tubulin binding / positive regulation of axonogenesis / cerebral cortex cell migration / negative regulation of neuron differentiation / positive regulation of Wnt signaling pathway ...forebrain ventricular zone progenitor cell division / cerebral cortex radially oriented cell migration / cell proliferation in forebrain / cerebellar cortex development / mitogen-activated protein kinase kinase kinase binding / gamma-tubulin binding / positive regulation of axonogenesis / cerebral cortex cell migration / negative regulation of neuron differentiation / positive regulation of Wnt signaling pathway / canonical Wnt signaling pathway / regulation of microtubule cytoskeleton organization / axon terminus / regulation of actin cytoskeleton organization / positive regulation of JNK cascade / actin binding / cytoskeleton / protein domain specific binding / focal adhesion / neuronal cell body / protein-containing complex / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Terawaki, S. / Shibata, N. / Higuchi, Y. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain. Authors: Terawaki, S.I. / Fujita, S. / Katsutani, T. / Shiomi, K. / Keino-Masu, K. / Masu, M. / Wakamatsu, K. / Shibata, N. / Higuchi, Y. #1: Journal: Nat. Struct. Mol. Biol. / Year: 2007 Title: The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization. Authors: Schwarz-Romond, T. / Fiedler, M. / Shibata, N. / Butler, P.J. / Kikuchi, A. / Higuchi, Y. / Bienz, M. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.4 KB | Display | ![]() |
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PDB format | ![]() | 99.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 484 KB | Display | ![]() |
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Full document | ![]() | 501.7 KB | Display | |
Data in XML | ![]() | 22 KB | Display | |
Data in CIF | ![]() | 30.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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Components
#1: Protein | Mass: 9783.971 Da / Num. of mol.: 7 / Fragment: UNP RESIDUES 625-707 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.33 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 0.1 M Na HEPES pH 7.8, 15%(v/v) ethylene glycol, 3%(v/v) glycerol, 4%(v/v) 1,3-propanediol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 20, 2009 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 14312 / % possible obs: 99 % / Redundancy: 6.2 % / Net I/σ(I): 16.3 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Bsol: 27.027 Å2 / ksol: 0.29 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3→29.088 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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