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- PDB-6rt4: The YTH domain of YTHDC1 protein in complex with m6ACU oligonucleotide -
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Open data
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Basic information
Entry | Database: PDB / ID: 6rt4 | ||||||
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Title | The YTH domain of YTHDC1 protein in complex with m6ACU oligonucleotide | ||||||
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![]() | RNA BINDING PROTEIN / Protein-RNA interaction / epitranscriptomics | ||||||
Function / homology | ![]() primary follicle stage / mRNA alternative polyadenylation / dosage compensation by inactivation of X chromosome / mRNA splice site recognition / N6-methyladenosine-containing RNA reader activity / regulation of mRNA splicing, via spliceosome / post-transcriptional regulation of gene expression / regulation of alternative mRNA splicing, via spliceosome / mRNA export from nucleus / mRNA splicing, via spliceosome ...primary follicle stage / mRNA alternative polyadenylation / dosage compensation by inactivation of X chromosome / mRNA splice site recognition / N6-methyladenosine-containing RNA reader activity / regulation of mRNA splicing, via spliceosome / post-transcriptional regulation of gene expression / regulation of alternative mRNA splicing, via spliceosome / mRNA export from nucleus / mRNA splicing, via spliceosome / spermatogenesis / in utero embryonic development / nuclear speck / mRNA binding / RNA binding / nucleoplasm / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bedi, R. / Sledz, P. / Caflisch, A. | ||||||
![]() | ![]() Title: Flexible Binding of m6A Reader Protein YTHDC1 to Its Preferred RNA Motif. Authors: Li, Y. / Bedi, R.K. / Wiedmer, L. / Huang, D. / Sledz, P. / Caflisch, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 90.7 KB | Display | ![]() |
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PDB format | ![]() | 65.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477.8 KB | Display | ![]() |
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Full document | ![]() | 479.3 KB | Display | |
Data in XML | ![]() | 18.2 KB | Display | |
Data in CIF | ![]() | 26.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6rt5C ![]() 6rt6C ![]() 6rt7C ![]() 4r3hS 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: RNA chain | Mass: 909.623 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #2: Protein | Mass: 18823.826 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.6 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 0.1 M Bis-Tris at pH 6.5, 0.2 M ammonium sulfate and 30% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 21, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.000002 Å / Relative weight: 1 |
Reflection | Resolution: 1.49→38.87 Å / Num. obs: 53214 / % possible obs: 95.1 % / Redundancy: 3.47 % / CC1/2: 0.999 / Rrim(I) all: 0.037 / Net I/σ(I): 17.15 |
Reflection shell | Resolution: 1.49→1.58 Å / Redundancy: 3.26 % / Mean I/σ(I) obs: 1.9 / Num. unique obs: 8210 / CC1/2: 0.885 / Rrim(I) all: 0.597 / % possible all: 93.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4R3H Resolution: 1.49→38.794 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 29.37
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.49→38.794 Å
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Refine LS restraints |
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LS refinement shell |
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