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Open data
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Basic information
Entry | Database: PDB / ID: 1stu | ||||||
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Title | DOUBLE STRANDED RNA BINDING DOMAIN | ||||||
![]() | MATERNAL EFFECT PROTEIN STAUFEN | ||||||
![]() | DOUBLE STRANDED RNA BINDING DOMAIN / STAUFEN | ||||||
Function / homology | ![]() germ plasm / subsynaptic reticulum / pole plasm RNA localization / bicoid mRNA localization / regulation of oskar mRNA translation / pole plasm protein localization / posterior cell cortex / regulation of pole plasm oskar mRNA localization / asymmetric protein localization involved in cell fate determination / anterograde dendritic transport of messenger ribonucleoprotein complex ...germ plasm / subsynaptic reticulum / pole plasm RNA localization / bicoid mRNA localization / regulation of oskar mRNA translation / pole plasm protein localization / posterior cell cortex / regulation of pole plasm oskar mRNA localization / asymmetric protein localization involved in cell fate determination / anterograde dendritic transport of messenger ribonucleoprotein complex / positive regulation of cytoplasmic mRNA processing body assembly / pole plasm assembly / neuroblast fate determination / positive regulation of synaptic assembly at neuromuscular junction / : / basal cortex / neuronal ribonucleoprotein granule / RNA localization / anterior/posterior axis specification, embryo / intracellular mRNA localization / apical cortex / protein localization to synapse / oogenesis / germ cell development / long-term memory / dendrite cytoplasm / basal plasma membrane / mRNA 3'-UTR binding / P-body / cytoplasmic ribonucleoprotein granule / cytoplasmic stress granule / double-stranded RNA binding / apical part of cell / cell cortex / neuron projection / apical plasma membrane / mRNA binding / neuronal cell body / RNA binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Bycroft, M. | ||||||
![]() | ![]() Title: NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. Authors: Bycroft, M. / Grunert, S. / Murzin, A.G. / Proctor, M. / St Johnston, D. #1: ![]() Title: A Conserved Double-Stranded RNA-Binding Domain Authors: Johnston, D.St. / Brown, N.H. / Gall, J.G. / Jantsch, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 423 KB | Display | ![]() |
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PDB format | ![]() | 352.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 343 KB | Display | ![]() |
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Full document | ![]() | 541.3 KB | Display | |
Data in XML | ![]() | 50.9 KB | Display | |
Data in CIF | ![]() | 76.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 7570.982 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: NMR, 20 STRUCTURES / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 20 |