+Open data
-Basic information
Entry | Database: PDB / ID: 3rzx | ||||||
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Title | Mouse importin alpha-Ku70 NLS peptide complex | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / Armadillo Repeats | ||||||
Function / homology | Function and homology information Ku70:Ku80 complex / positive regulation of lymphocyte differentiation / DNA-dependent protein kinase complex / Sensing of DNA Double Strand Breaks / DNA-dependent protein kinase-DNA ligase 4 complex / entry of viral genome into host nucleus through nuclear pore complex via importin / cellular response to X-ray / nonhomologous end joining complex / positive regulation of viral life cycle / DNA ligation ...Ku70:Ku80 complex / positive regulation of lymphocyte differentiation / DNA-dependent protein kinase complex / Sensing of DNA Double Strand Breaks / DNA-dependent protein kinase-DNA ligase 4 complex / entry of viral genome into host nucleus through nuclear pore complex via importin / cellular response to X-ray / nonhomologous end joining complex / positive regulation of viral life cycle / DNA ligation / nuclear telomere cap complex / regulation of smooth muscle cell proliferation / Cytosolic sensors of pathogen-associated DNA / double-strand break repair via classical nonhomologous end joining / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / IRF3-mediated induction of type I IFN / host cell / recombinational repair / nuclear import signal receptor activity / nuclear localization sequence binding / cellular hyperosmotic salinity response / NLS-bearing protein import into nucleus / telomeric DNA binding / 2-LTR circle formation / Lyases; Carbon-oxygen lyases; Other carbon-oxygen lyases / 5'-deoxyribose-5-phosphate lyase activity / positive regulation of protein kinase activity / ATP-dependent activity, acting on DNA / DNA helicase activity / telomere maintenance / activation of innate immune response / cyclin binding / protein-DNA complex / Nonhomologous End-Joining (NHEJ) / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cellular response to gamma radiation / double-strand break repair via nonhomologous end joining / cytoplasmic stress granule / protein import into nucleus / histone deacetylase binding / double-stranded DNA binding / scaffold protein binding / nuclear membrane / secretory granule lumen / DNA-binding transcription factor binding / ficolin-1-rich granule lumen / transcription regulator complex / postsynaptic density / damaged DNA binding / chromosome, telomeric region / transcription cis-regulatory region binding / innate immune response / negative regulation of DNA-templated transcription / glutamatergic synapse / Neutrophil degranulation / protein-containing complex binding / nucleolus / positive regulation of DNA-templated transcription / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / RNA binding / extracellular region / nucleoplasm / ATP binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.61 Å | ||||||
Authors | Takeda, A.A.S. / Fontes, M.R.M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2011 Title: Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80. Authors: Takeda, A.A. / de Barros, A.C. / Chang, C.W. / Kobe, B. / Fontes, M.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3rzx.cif.gz | 99.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3rzx.ent.gz | 73.8 KB | Display | PDB format |
PDBx/mmJSON format | 3rzx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rz/3rzx ftp://data.pdbj.org/pub/pdb/validation_reports/rz/3rzx | HTTPS FTP |
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-Related structure data
Related structure data | 3rz9C 1pjnS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 55330.566 Da / Num. of mol.: 1 / Fragment: NLS binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kpna2, Rch1 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P52293 |
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#2: Protein/peptide | Mass: 2474.772 Da / Num. of mol.: 1 / Fragment: Nuclear localization signal / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P12956 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 59.81 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: LNLS / Beamline: W01B-MX2 / Wavelength: 1.45859 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 27, 2008 / Details: SAGITALLY FOCUSED Si(111) |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.45859 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→29.07 Å / Num. all: 22152 / Num. obs: 20974 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.6→2.69 Å / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1PJN Resolution: 2.61→29.07 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.933 / SU B: 7.332 / SU ML: 0.157 / Cross valid method: THROUGHOUT / ESU R: 0.3 / ESU R Free: 0.238 / 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: 53.172 Å2
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Refinement step | Cycle: LAST / Resolution: 2.61→29.07 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.61→2.674 Å / Total num. of bins used: 20
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