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Open data
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Basic information
Entry | Database: PDB / ID: 4j0u | ||||||
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Title | Crystal structure of IFIT5/ISG58 | ||||||
![]() | Interferon-induced protein with tetratricopeptide repeats 5 | ||||||
![]() | RNA BINDING PROTEIN / IFIT5 structure / helix / antiviral | ||||||
Function / homology | ![]() RNA cap binding / poly(U) RNA binding / negative regulation of viral genome replication / ruffle membrane / Interferon alpha/beta signaling / actin cytoskeleton / apical part of cell / double-stranded DNA binding / positive regulation of canonical NF-kappaB signal transduction / defense response to virus ...RNA cap binding / poly(U) RNA binding / negative regulation of viral genome replication / ruffle membrane / Interferon alpha/beta signaling / actin cytoskeleton / apical part of cell / double-stranded DNA binding / positive regulation of canonical NF-kappaB signal transduction / defense response to virus / tRNA binding / single-stranded RNA binding / innate immune response / RNA binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liu, Y. / Liang, H. / Feng, F. / Yuan, L. / Wang, Y.E. / Crowley, C. / Lv, Z. / Li, J. / Zeng, S. / Cheng, G. | ||||||
![]() | ![]() Title: Crystal Structure of IFIT5 Authors: Liu, Y. / Liang, H. / Feng, F. / Yuan, L. / Wang, Y.E. / Crowley, C. / Lv, Z. / Li, J. / Zeng, S. / Cheng, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 110.6 KB | Display | ![]() |
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PDB format | ![]() | 89.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 427 KB | Display | ![]() |
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Full document | ![]() | 435.1 KB | Display | |
Data in XML | ![]() | 22 KB | Display | |
Data in CIF | ![]() | 33 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 55933.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.74 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: 100mM HEPES, 150mM NaCl, 8% PEG3350, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.969→50 Å / Num. all: 37989 / Num. obs: 37930 / % possible obs: 99 % / Observed criterion σ(F): 2.2 / Observed criterion σ(I): 4.8 / Biso Wilson estimate: 28.85 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 49.666 Å2 / ksol: 0.348 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 172.84 Å2 / Biso mean: 39.7091 Å2 / Biso min: 15.66 Å2
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Refinement step | Cycle: LAST / Resolution: 1.969→36.725 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: 14
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