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- PDB-2l3j: The solution structure of the ADAR2 dsRBM-RNA complex reveals a s... -
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Basic information
Entry | Database: PDB / ID: 2l3j | ||||||
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Title | The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific read out of the minor groove | ||||||
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![]() | Hydrolase/RNA / editing / dsRNA recognition / dsRBM / Hydrolase-RNA complex | ||||||
Function / homology | ![]() 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 behavior / motor neuron apoptotic process / 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 / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Stefl, R. / Oberstrass, F.C. / Allain, F.H.-T. | ||||||
![]() | ![]() Title: The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove. Authors: Stefl, R. / Oberstrass, F.C. / Hood, J.L. / Jourdan, M. / Zimmermann, M. / Skrisovska, L. / Maris, C. / Peng, L. / Hofr, C. / Emeson, R.B. / Allain, F.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2 MB | Display | ![]() |
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PDB format | ![]() | 1.7 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 390.7 KB | Display | ![]() |
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Full document | ![]() | 623.6 KB | Display | |
Data in XML | ![]() | 103.1 KB | Display | |
Data in CIF | ![]() | 146.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 25447.760 Da / Num. of mol.: 1 / Fragment: UNP residues 74-301 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P51400, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds |
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#2: RNA chain | Mass: 22788.502 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1 mM [U-100% 15N] entity_1-1, 1 mM RNA (71-MER)-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 7.6 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 19 |