+Open data
-Basic information
Entry | Database: PDB / ID: 1wsp | ||||||
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Title | Crystal structure of axin dix domain | ||||||
Components | Axin 1 proteinAXIN1 | ||||||
Keywords | SIGNALING PROTEIN | ||||||
Function / homology | Function and homology information Beta-catenin phosphorylation cascade / Disassembly of the destruction complex and recruitment of AXIN to the membrane / TCF dependent signaling in response to WNT / Degradation of beta-catenin by the destruction complex / Degradation of AXIN / embryonic skeletal joint morphogenesis / armadillo repeat domain binding / hemoglobin metabolic process / response to quercetin / head development ...Beta-catenin phosphorylation cascade / Disassembly of the destruction complex and recruitment of AXIN to the membrane / TCF dependent signaling in response to WNT / Degradation of beta-catenin by the destruction complex / Degradation of AXIN / embryonic skeletal joint morphogenesis / armadillo repeat domain binding / hemoglobin metabolic process / response to quercetin / head development / cell development / Ub-specific processing proteases / dorsal/ventral axis specification / axial mesoderm formation / axial mesoderm development / post-anal tail morphogenesis / epigenetic programming in the zygotic pronuclei / beta-catenin destruction complex / positive regulation of ubiquitin-dependent protein catabolic process / nervous system process / dorsal/ventral pattern formation / I-SMAD binding / Wnt signalosome / adult walking behavior / regulation of canonical Wnt signaling pathway / erythrocyte homeostasis / nucleocytoplasmic transport / negative regulation of protein metabolic process / negative regulation of fat cell differentiation / negative regulation of Wnt signaling pathway / negative regulation of transcription elongation by RNA polymerase II / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / R-SMAD binding / ubiquitin-like ligase-substrate adaptor activity / canonical Wnt signaling pathway / lateral plasma membrane / cytoplasmic microtubule organization / positive regulation of peptidyl-threonine phosphorylation / positive regulation of protein ubiquitination / cell periphery / sensory perception of sound / positive regulation of JNK cascade / regulation of protein phosphorylation / protein catabolic process / negative regulation of canonical Wnt signaling pathway / beta-catenin binding / Wnt signaling pathway / protein polyubiquitination / positive regulation of protein catabolic process / : / microtubule cytoskeleton / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / p53 binding / positive regulation of peptidyl-serine phosphorylation / cell cortex / cytoplasmic vesicle / protein-containing complex assembly / in utero embryonic development / molecular adaptor activity / positive regulation of protein phosphorylation / protein domain specific binding / negative regulation of gene expression / signaling receptor binding / synapse / apoptotic process / ubiquitin protein ligase binding / protein kinase binding / perinuclear region of cytoplasm / enzyme binding / protein homodimerization activity / protein-containing complex / identical protein binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.9 Å | ||||||
Authors | Shibata, N. / Hanamura, T. / Yamamoto, R. / Ueda, Y. / Yamamoto, H. / Kikuchi, A. / Higuchi, Y. | ||||||
Citation | Journal: to be published Title: Crystal structure of axin dix domain Authors: Shibata, N. / Hanamura, T. / Yamamoto, R. / Ueda, Y. / Yamamoto, H. / Kikuchi, A. / Higuchi, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wsp.cif.gz | 68.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wsp.ent.gz | 51.6 KB | Display | PDB format |
PDBx/mmJSON format | 1wsp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ws/1wsp ftp://data.pdbj.org/pub/pdb/validation_reports/ws/1wsp | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | Each one of the chains (A, B, and C) is the minimum biological unit. |
-Components
#1: Protein | Mass: 9734.206 Da / Num. of mol.: 3 / Fragment: DIX DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pMALc2 / Production host: Escherichia coli (E. coli) / References: GenBank: 2982198, UniProt: O70239*PLUS #2: Chemical | ChemComp-HG / #3: Chemical | ChemComp-BEZ / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.33 Å3/Da / Density % sol: 63 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion / pH: 7.5 / Details: PEG8000, pH 7.5, VAPOR DIFFUSION, temperature 283K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 10, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.9→58.772 Å / Num. all: 9245 / Num. obs: 9237 / % possible obs: 100 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 7.2 % / Biso Wilson estimate: 157 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 2.9→3.06 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.224 / Mean I/σ(I) obs: 3.3 / Num. unique all: 1335 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.9→29.17 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 1214210.2 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 73.362 Å2 / ksol: 0.326264 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.9→29.17 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: CONSTR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→3 Å / Rfactor Rfree error: 0.044 / Total num. of bins used: 10
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Xplor file |
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