+Open data
-Basic information
Entry | Database: PDB / ID: 5uzn | ||||||
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Title | Crystal structure of Glorund qRRM3 domain | ||||||
Components | AT27789p | ||||||
Keywords | RNA BINDING PROTEIN / quasi-RNA recognition motif / qRRM | ||||||
Function / homology | Function and homology information maternal specification of dorsal/ventral axis, oocyte, germ-line encoded / intracellular mRNA localization involved in pattern specification process / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / pole plasm oskar mRNA localization / regulation of RNA splicing / chromosome organization / wound healing / regulation of translation / ribonucleoprotein complex ...maternal specification of dorsal/ventral axis, oocyte, germ-line encoded / intracellular mRNA localization involved in pattern specification process / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / pole plasm oskar mRNA localization / regulation of RNA splicing / chromosome organization / wound healing / regulation of translation / ribonucleoprotein complex / mRNA binding / protein-containing complex / RNA binding / nucleoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.99 Å | ||||||
Authors | Teramoto, T. / Hall, T.M.T. | ||||||
Citation | Journal: Cell Rep / Year: 2017 Title: The Drosophila hnRNP F/H Homolog Glorund Uses Two Distinct RNA-Binding Modes to Diversify Target Recognition. Authors: Tamayo, J.V. / Teramoto, T. / Chatterjee, S. / Hall, T.M. / Gavis, E.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5uzn.cif.gz | 32.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5uzn.ent.gz | 20.1 KB | Display | PDB format |
PDBx/mmJSON format | 5uzn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5uzn_validation.pdf.gz | 443.4 KB | Display | wwPDB validaton report |
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Full document | 5uzn_full_validation.pdf.gz | 443.5 KB | Display | |
Data in XML | 5uzn_validation.xml.gz | 6.1 KB | Display | |
Data in CIF | 5uzn_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/5uzn ftp://data.pdbj.org/pub/pdb/validation_reports/uz/5uzn | HTTPS FTP |
-Related structure data
Related structure data | 5uzgC 5uzmC 2kg1S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 10782.001 Da / Num. of mol.: 1 / Fragment: qRRM3 domain residues 475-562 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: glo, CG6946, Dmel_CG6946 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9VGH5 | ||||
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#2: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.52 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.5 M ammonium sulfate, 0.1 M Na cacodylate pH 6.4, 1.0 M lithium sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å |
Detector | Type: RIGAKU SATURN 92 / Detector: CCD / Date: Sep 4, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→50 Å / Num. obs: 6462 / % possible obs: 95.9 % / Redundancy: 12.5 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 32.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2KG1 Resolution: 1.99→24.809 Å / SU ML: 0.18 / Cross valid method: NONE / σ(F): 0.69 / Phase error: 19.5
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.99→24.809 Å
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Refine LS restraints |
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LS refinement shell |
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