+Open data
-Basic information
Entry | Database: PDB / ID: 5klt | ||||||
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Title | Prototypical P4[M]cNLS | ||||||
Components |
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Keywords | PROTEIN TRANSPORT/Viral protein / Importin alpha / Complex / nuclear localisation signal / PROTEIN TRANSPORT-Viral protein complex | ||||||
Function / homology | Function and homology information Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / host cell / cytoplasmic stress granule ...Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / host cell / cytoplasmic stress granule / protein import into nucleus / histone deacetylase binding / nuclear membrane / DNA-binding transcription factor binding / postsynaptic density / glutamatergic synapse / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Smith, K.M. / Forwood, J.K. | ||||||
Citation | Journal: Biochim Biophys Acta Mol Cell Res / Year: 2018 Title: Contribution of the residue at position 4 within classical nuclear localization signals to modulating interaction with importins and nuclear targeting. Authors: Smith, K.M. / Di Antonio, V. / Bellucci, L. / Thomas, D.R. / Caporuscio, F. / Ciccarese, F. / Ghassabian, H. / Wagstaff, K.M. / Forwood, J.K. / Jans, D.A. / Palu, G. / Alvisi, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5klt.cif.gz | 170.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5klt.ent.gz | 135.1 KB | Display | PDB format |
PDBx/mmJSON format | 5klt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kl/5klt ftp://data.pdbj.org/pub/pdb/validation_reports/kl/5klt | HTTPS FTP |
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-Related structure data
Related structure data | 5klrC 3ul1S C: citing same article (ref.) S: Starting model for refinement |
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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: 55268.473 Da / Num. of mol.: 1 / Fragment: UNp residues 70-529 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kpna2, Rch1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P52293 |
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#2: Protein/peptide | Mass: 1696.084 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli BL21(DE3) (bacteria) |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.09 Å3/Da / Density % sol: 60.24 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 1M Sodium citrate pH6, 10mM DTT |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å | |||||||||||||||
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Sep 26, 2015 | |||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 | |||||||||||||||
Reflection | Resolution: 2.6→26.7 Å / Num. obs: 22383 / % possible obs: 99.9 % / Redundancy: 14.1 % / Biso Wilson estimate: 34.34 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.3 / Net I/σ(I): 9.3 | |||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3UL1 Resolution: 2.6→26.698 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.18
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 132.09 Å2 / Biso mean: 44.5811 Å2 / Biso min: 19.17 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.6→26.698 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: 8 / % reflection obs: 100 %
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