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Open data
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Basic information
Entry | Database: PDB / ID: 6s8r | ||||||
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Title | D. melanogaster RNA helicase Me31B in complex with GIGYF | ||||||
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Function / homology | ![]() positive regulation of post-transcriptional gene silencing / sensory dendrite / translation repressor complex / : / regulation of olfactory learning / mRNA decay by 5' to 3' exoribonuclease / regulation of neuron projection arborization / follicle cell of egg chamber development / : / pole cell formation ...positive regulation of post-transcriptional gene silencing / sensory dendrite / translation repressor complex / : / regulation of olfactory learning / mRNA decay by 5' to 3' exoribonuclease / regulation of neuron projection arborization / follicle cell of egg chamber development / : / pole cell formation / neuronal ribonucleoprotein granule / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Peter, D. / Valkov, E. | ||||||
![]() | ![]() Title: Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated translational repression. Authors: Peter, D. / Ruscica, V. / Bawankar, P. / Weber, R. / Helms, S. / Valkov, E. / Igreja, C. / Izaurralde, 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 | ![]() | 65 KB | Display | ![]() |
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PDB format | ![]() | 38.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6s8sC ![]() 5anrS 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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Unit cell |
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Components
#1: Protein | Mass: 20004.273 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 2847.999 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-ACT / ![]() #4: Water | ChemComp-HOH / | ![]() Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.84 % |
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Crystal grow![]() | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.1 M sodium acetate (pH 5.0), 0.15 M ammonium chloride, 16% (w/v) PEG 6000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 30, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.4→42 Å / Num. obs: 7712 / % possible obs: 95.8 % / Redundancy: 10.4 % / Biso Wilson estimate: 27.21 Å2 / Rsym value: 0.188 / Net I/σ(I): 8.91 |
Reflection shell | Resolution: 2.4→2.46 Å / Redundancy: 9.7 % / Num. unique obs: 522 / Rsym value: 1.06 / % possible all: 88.5 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 5ANR Resolution: 2.41→39.7 Å / SU ML: 0.2761 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 26.1878
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.19 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.41→39.7 Å
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Refine LS restraints |
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LS refinement shell |
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