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- PDB-1iq1: CRYSTAL STRUCTURE OF THE IMPORTIN-ALPHA(44-54)-IMPORTIN-ALPHA(70-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1iq1 | ||||||
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Title | CRYSTAL STRUCTURE OF THE IMPORTIN-ALPHA(44-54)-IMPORTIN-ALPHA(70-529) COMPLEX | ||||||
![]() | (IMPORTIN ALPHA-2 SUBUNIT) x 2 | ||||||
![]() | PROTEIN TRANSPORT / armadillo repeat / solenoid / autoinhibition | ||||||
Function / homology | ![]() 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 / cytoplasmic stress granule / protein import into nucleus ...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 / cytoplasmic stress granule / protein import into nucleus / host cell / DNA-binding transcription factor binding / postsynaptic density / glutamatergic synapse / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Catimel, B. / Teh, T. / Fontes, M.R.M. / Jennings, I.G. / Kobe, B. | ||||||
![]() | ![]() Title: Biophysical characterization of interactions involving importin-alpha during nuclear import. Authors: Catimel, B. / Teh, T. / Fontes, M.R. / Jennings, I.G. / Jans, D.A. / Howlett, G.J. / Nice, E.C. / Kobe, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 97.7 KB | Display | ![]() |
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PDB format | ![]() | 73.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 380.4 KB | Display | ![]() |
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Full document | ![]() | 393 KB | Display | |
Data in XML | ![]() | 11.1 KB | Display | |
Data in CIF | ![]() | 16.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ialS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein/peptide | Mass: 1364.552 Da / Num. of mol.: 2 / Fragment: AUTOINHIBITORY PEPTIDE(RESIDUES 44-54) / Source method: obtained synthetically / Details: peptide synthesis / References: UniProt: P52293 #2: Protein | | Mass: 49886.633 Da / Num. of mol.: 1 / Fragment: ARMADILLO REPEAT DOMAIN(RESIDUES 70-529) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.37 Å3/Da / Density % sol: 63.53 % | ||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: sodium phosphate, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / Details: Fontes, M.R.M., (2000) J. Mol. Biol., 297, 1183. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1999 |
Radiation | Monochromator: Mirror optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 17671 / % possible obs: 97.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.8 % / Rmerge(I) obs: 0.124 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 0.561 / Mean I/σ(I) obs: 1.3 / % possible all: 96.9 |
Reflection | *PLUS Num. obs: 18165 / % possible obs: 97.6 % / Num. measured all: 142209 |
Reflection shell | *PLUS % possible obs: 96.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1IAL Resolution: 2.8→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 30 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.209 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.2 | ||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å / Rfactor Rfree: 0.335 / Rfactor Rwork: 0.315 / Rfactor obs: 0.315 |