[English] 日本語
Yorodumi- PDB-1emu: STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1emu | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE OF THE AXIN RGS-HOMOLOGOUS DOMAIN IN COMPLEX WITH A SAMP REPEAT FROM APC | ||||||
Components |
| ||||||
Keywords | SIGNALING PROTEIN / RGS domain | ||||||
Function / homology | Function and homology information APC truncation mutants are not K63 polyubiquitinated / armadillo repeat domain binding / regulation of microtubule-based movement / head development / negative regulation of cell cycle G1/S phase transition / cell development / dorsal/ventral axis specification / axial mesoderm formation / gamma-catenin binding / regulation of attachment of spindle microtubules to kinetochore ...APC truncation mutants are not K63 polyubiquitinated / armadillo repeat domain binding / regulation of microtubule-based movement / head development / negative regulation of cell cycle G1/S phase transition / cell development / dorsal/ventral axis specification / axial mesoderm formation / gamma-catenin binding / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly / positive regulation of protein localization to centrosome / pattern specification process / bicellular tight junction assembly / protein kinase regulator activity / post-anal tail morphogenesis / negative regulation of microtubule depolymerization / negative regulation of cyclin-dependent protein serine/threonine kinase activity / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / microtubule plus-end binding / epigenetic programming in the zygotic pronuclei / beta-catenin destruction complex / positive regulation of ubiquitin-dependent protein catabolic process / regulation of microtubule-based process / heart valve development / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / catenin complex / I-SMAD binding / negative regulation of protein metabolic process / Wnt signalosome / Disassembly of the destruction complex and recruitment of AXIN to the membrane / cell fate specification / nucleocytoplasmic transport / endocardial cushion morphogenesis / negative regulation of fat cell differentiation / dynein complex binding / negative regulation of G1/S transition of mitotic cell cycle / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / mitotic spindle assembly checkpoint signaling / Apoptotic cleavage of cellular proteins / regulation of cell differentiation / negative regulation of transcription elongation by RNA polymerase II / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / activation of protein kinase activity / R-SMAD binding / mitotic cytokinesis / ubiquitin-like ligase-substrate adaptor activity / bicellular tight junction / canonical Wnt signaling pathway / lateral plasma membrane / signaling adaptor activity / cytoplasmic microtubule organization / positive regulation of peptidyl-threonine phosphorylation / positive regulation of protein ubiquitination / TCF dependent signaling in response to WNT / cell periphery / Deactivation of the beta-catenin transactivating complex / Degradation of AXIN / sensory perception of sound / adherens junction / positive regulation of JNK cascade / negative regulation of canonical Wnt signaling pathway / Degradation of beta-catenin by the destruction complex / kinetochore / ruffle membrane / beta-catenin binding / Wnt signaling pathway / protein polyubiquitination / positive regulation of protein catabolic process / : / microtubule cytoskeleton / cell migration / Ovarian tumor domain proteases / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / p53 binding / lamellipodium / insulin receptor signaling pathway / positive regulation of peptidyl-serine phosphorylation / nervous system development / positive regulation of cold-induced thermogenesis / cell cortex / cytoplasmic vesicle / microtubule binding / proteasome-mediated ubiquitin-dependent protein catabolic process / protein-containing complex assembly / Estrogen-dependent gene expression / in utero embryonic development / microtubule / molecular adaptor activity / Ub-specific processing proteases / cell adhesion Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å | ||||||
Authors | Spink, K.E. / Polakis, P. / Weis, W.I. | ||||||
Citation | Journal: EMBO J. / Year: 2000 Title: Structural basis of the Axin-adenomatous polyposis coli interaction. Authors: Spink, K.E. / Polakis, P. / Weis, W.I. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1emu.cif.gz | 44.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1emu.ent.gz | 32.1 KB | Display | PDB format |
PDBx/mmJSON format | 1emu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/em/1emu ftp://data.pdbj.org/pub/pdb/validation_reports/em/1emu | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 15349.550 Da / Num. of mol.: 1 / Fragment: RGS-HOMOLOGOUS DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX-2T / Production host: Bacteria (eubacteria) / References: UniProt: O15169 | ||
---|---|---|---|
#2: Protein/peptide | Mass: 1766.965 Da / Num. of mol.: 1 / Fragment: THIRD SAMP REPEAT / Source method: obtained synthetically Details: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED BY FMOC METHOD. THE SEQUENCE OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS) References: UniProt: P25054 | ||
#3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
---|
-Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.33 % | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: MES, PEG 400, glycerol, DTT, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source |
| |||||||||||||||
Detector |
| |||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
| |||||||||||||||
Reflection | Resolution: 1.9→32 Å / Num. obs: 12617 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 14.9 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 19.3 | |||||||||||||||
Reflection shell | Resolution: 1.9→1.93 Å / Redundancy: 3 % / Rmerge(I) obs: 0.295 / Num. unique all: 611 / % possible all: 99.7 | |||||||||||||||
Reflection shell | *PLUS % possible obs: 99.7 % |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.9→32 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 11160027.33 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.02 Å2 / ksol: 0.389 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.4 Å2
| ||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→32 Å
| ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.5 / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|