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Open data
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Basic information
Entry | Database: PDB / ID: 5nvl | ||||||
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Title | Crystal structure of the human 4EHP-GIGYF2 complex | ||||||
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![]() | TRANSLATION / translational regulation / cap-binding protein / 4EHP-binding protein / GRB10-interacting GYF protein 2 | ||||||
Function / homology | ![]() musculoskeletal movement / post-transcriptional gene silencing / spinal cord motor neuron differentiation / proximal dendrite / RNA cap binding / eukaryotic translation initiation factor 4F complex / translation factor activity, RNA binding / mRNA cap binding / miRNA-mediated gene silencing by inhibition of translation / RNA 7-methylguanosine cap binding ...musculoskeletal movement / post-transcriptional gene silencing / spinal cord motor neuron differentiation / proximal dendrite / RNA cap binding / eukaryotic translation initiation factor 4F complex / translation factor activity, RNA binding / mRNA cap binding / miRNA-mediated gene silencing by inhibition of translation / RNA 7-methylguanosine cap binding / feeding behavior / proline-rich region binding / negative regulation of type I interferon-mediated signaling pathway / mRNA destabilization / neuromuscular process controlling balance / negative regulation of translational initiation / homeostasis of number of cells within a tissue / mitotic G1 DNA damage checkpoint signaling / translational initiation / translation initiation factor activity / rescue of stalled ribosome / adult locomotory behavior / insulin-like growth factor receptor signaling pathway / post-embryonic development / P-body / multicellular organism growth / ISG15 antiviral mechanism / cytoplasmic stress granule / perikaryon / vesicle / molecular adaptor activity / negative regulation of translation / endosome / cadherin binding / ubiquitin protein ligase binding / Golgi apparatus / endoplasmic reticulum / protein-containing complex / RNA binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Peter, D. / Valkov, E. | ||||||
![]() | ![]() Title: GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression. Authors: Peter, D. / Weber, R. / Sandmeir, F. / Wohlbold, L. / Helms, S. / Bawankar, P. / Valkov, E. / Igreja, C. / Izaurralde, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 279.7 KB | Display | ![]() |
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PDB format | ![]() | 234.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 442.4 KB | Display | ![]() |
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Full document | ![]() | 444.7 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 23.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nvkC ![]() 5nvmC ![]() 5nvnC ![]() 2jgbS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21979.102 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: the first 5 residues of the coordinate sequence of chain A and the first residue of the coordinate sequence of chain C belong to the expression tag Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 8689.040 Da / Num. of mol.: 2 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: 2.06 Å3/Da / Density % sol: 40.35 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.1 M sodium citrate pH 5.0 0.1 M magnesium chloride 12% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 19, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00001 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→45.9 Å / Num. obs: 23500 / % possible obs: 99.8 % / Redundancy: 11.2 % / Rsym value: 0.125 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 2.3→2.36 Å / Redundancy: 10.6 % / Mean I/σ(I) obs: 2.06 / Num. unique all: 1690 / Rsym value: 0.938 / % possible all: 98.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2JGB Resolution: 2.3→45.888 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 27.9
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 62 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→45.888 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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