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- PDB-5ctt: Crystal structure of human SART3/TIP110 NLS-mouse importin alpha ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ctt | ||||||
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Title | Crystal structure of human SART3/TIP110 NLS-mouse importin alpha complex | ||||||
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![]() | TRANSPORT PROTEIN / IMMUNE SYSTEM / NUCLEAR PROTEIN / RNA BINDING PROTEIN / Nuclear localization signal / Complex / Protein Transporter | ||||||
Function / homology | ![]() U6atac snRNA binding / ASAP complex / 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 / U4 snRNA binding / nuclear import signal receptor activity / hematopoietic stem cell proliferation ...U6atac snRNA binding / ASAP complex / 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 / U4 snRNA binding / nuclear import signal receptor activity / hematopoietic stem cell proliferation / transcription elongation-coupled chromatin remodeling / nuclear localization sequence binding / NLS-bearing protein import into nucleus / ubiquitin-specific protease binding / homeostasis of number of cells / spliceosomal tri-snRNP complex assembly / U6 snRNA binding / spliceosomal snRNP assembly / Cajal body / cell morphogenesis / mRNA splicing, via spliceosome / cytoplasmic stress granule / protein import into nucleus / host cell / nucleosome assembly / histone binding / regulation of gene expression / DNA-binding transcription factor binding / postsynaptic density / nuclear speck / glutamatergic synapse / RNA binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Park, J.K. / Kim, E.E. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for recruiting and shuttling of the spliceosomal deubiquitinase USP4 by SART3 Authors: Park, J.K. / Das, T. / Song, E.J. / Kim, E.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 112.4 KB | Display | ![]() |
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PDB format | ![]() | 82.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 442.6 KB | Display | ![]() |
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Full document | ![]() | 447.6 KB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 34.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ctqC ![]() 5ctrC ![]() 1ialS C: citing same article ( 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 | Mass: 48446.379 Da / Num. of mol.: 1 / Fragment: UNP residues 72-497 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 6535.394 Da / Num. of mol.: 1 / Fragment: UNP residues 601-649 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.17 Å3/Da / Density % sol: 65.97 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 100mM HEPES, pH 6.6, 1.6M sodium citrate, 10mM DTT |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 5, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 77648 / % possible obs: 99 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 2 % / Rmerge(I) obs: 0.453 / Mean I/σ(I) obs: 1.96 / % possible all: 97.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1IAL Resolution: 1.7→37.765 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.44 / Phase error: 21.42 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 1.24 Å / VDW probe radii: 1.4 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 36.684 Å2 / ksol: 0.341 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.7→37.765 Å
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Refine LS restraints |
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LS refinement shell |
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