+Open data
-Basic information
Entry | Database: PDB / ID: 6bvz | ||||||
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Title | Importin alpha 3 in cargo free state | ||||||
Components | Importin subunit alpha-3 | ||||||
Keywords | TRANSPORT PROTEIN / Importin / Karyopherin / Nuclear transport | ||||||
Function / homology | Function and homology information dopamine secretion / NS1 Mediated Effects on Host Pathways / NLS-dependent protein nuclear import complex / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nuclear pore / ISG15 antiviral mechanism / protein import into nucleus / gene expression ...dopamine secretion / NS1 Mediated Effects on Host Pathways / NLS-dependent protein nuclear import complex / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nuclear pore / ISG15 antiviral mechanism / protein import into nucleus / gene expression / nuclear membrane / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Smith, K.M. / Tsimbalyuk, S. / Edwards, M.R. / Aragao, D. / Cross, E.M. / Basler, C.F. / Forwood, J.K. | ||||||
Funding support | Australia, 1items
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Citation | Journal: Nat Commun / Year: 2018 Title: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. Authors: Smith, K.M. / Tsimbalyuk, S. / Edwards, M.R. / Cross, E.M. / Batra, J. / Soares da Costa, T.P. / Aragao, D. / Basler, C.F. / Forwood, J.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6bvz.cif.gz | 88.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6bvz.ent.gz | 68.4 KB | Display | PDB format |
PDBx/mmJSON format | 6bvz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bv/6bvz ftp://data.pdbj.org/pub/pdb/validation_reports/bv/6bvz | HTTPS FTP |
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-Related structure data
Related structure data | 6bvtC 6bvvC 6bw0C 6bw1C 6bw9C 6bwaC 6bwbC 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: 50325.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KPNA4, QIP1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O00629 |
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#2: 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: 2.27 Å3/Da / Density % sol: 45.87 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2 M sodium nitrate, 0.1 M bis-tris propane pH 6.5, 25% w/v PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 13, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→19.814 Å / Num. obs: 19290 / % possible obs: 95 % / Redundancy: 5.5 % / CC1/2: 0.977 / Rpim(I) all: 0.086 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 1.8 / Num. unique obs: 1942 / CC1/2: 0.785 / Rpim(I) all: 0.304 / % possible all: 98.2 |
-Processing
Software |
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Refinement | Resolution: 2.3→19.814 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 28.93
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→19.814 Å
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Refine LS restraints |
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LS refinement shell |
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