+Open data
-Basic information
Entry | Database: PDB / ID: 2b7t | ||||||
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Title | Structure of ADAR2 dsRBM1 | ||||||
Components | Double-stranded RNA-specific editase 1 | ||||||
Keywords | HYDROLASE / RNA editing / RNA-binding protein | ||||||
Function / homology | Function and homology information C6 deamination of adenosine / Formation of editosomes by ADAR proteins / positive regulation of mRNA processing / hypoglossal nerve morphogenesis / muscle tissue morphogenesis / facial nerve morphogenesis / spinal cord ventral commissure morphogenesis / double-stranded RNA adenine deaminase / tRNA-specific adenosine deaminase activity / mRNA modification ...C6 deamination of adenosine / Formation of editosomes by ADAR proteins / positive regulation of mRNA processing / hypoglossal nerve morphogenesis / muscle tissue morphogenesis / facial nerve morphogenesis / spinal cord ventral commissure morphogenesis / double-stranded RNA adenine deaminase / tRNA-specific adenosine deaminase activity / mRNA modification / double-stranded RNA adenosine deaminase activity / negative regulation of protein kinase activity by regulation of protein phosphorylation / base conversion or substitution editing / neuromuscular process controlling posture / adenosine to inosine editing / neuromuscular synaptic transmission / innervation / motor neuron apoptotic process / motor behavior / positive regulation of viral genome replication / RNA processing / negative regulation of cell migration / multicellular organism growth / mRNA processing / double-stranded RNA binding / regulation of cell cycle / negative regulation of cell population proliferation / synapse / nucleolus / RNA binding / nucleoplasm / identical protein binding / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Stefl, R. / Xu, M. / Skrisovska, L. / Emeson, R.B. / Allain, F.H.-T. | ||||||
Citation | Journal: Structure / Year: 2006 Title: Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. Authors: Stefl, R. / Xu, M. / Skrisovska, L. / Emeson, R.B. / Allain, F.H.-T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2b7t.cif.gz | 442.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2b7t.ent.gz | 372.2 KB | Display | PDB format |
PDBx/mmJSON format | 2b7t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b7/2b7t ftp://data.pdbj.org/pub/pdb/validation_reports/b7/2b7t | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7922.332 Da / Num. of mol.: 1 / Fragment: double-stranded RNA-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Adarb1, Red1 / Plasmid: pET16 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P51400, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 250mM total salt / pH: 8.0 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: DYANA, SPARKY, Amber / Version: 7 / Developer: Case, D.A., et al. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20 |