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Open data
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Basic information
Entry | Database: PDB / ID: 5fgo | ||||||
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Title | Crystal structure of D. melanogaster Pur-alpha repeat III. | ||||||
![]() | CG1507-PB, isoform B | ||||||
![]() | DNA BINDING PROTEIN / DNA-protein interaction / RNA-protein interaction / DNA unwinding / FXTAS / ALS / FTLD / 5q31.3 microdeletion syndrome / neurodegeneration | ||||||
Function / homology | ![]() purine-rich negative regulatory element binding / RNA polymerase II transcription regulatory region sequence-specific DNA binding / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / mRNA binding / regulation of transcription by RNA polymerase II / DNA binding / RNA binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Windhager, A. / Janowski, R. / Niessing, D. | ||||||
![]() | ![]() Title: Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alpha. Authors: Weber, J. / Bao, H. / Hartlmuller, C. / Wang, Z. / Windhager, A. / Janowski, R. / Madl, T. / Jin, P. / Niessing, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 99.1 KB | Display | ![]() |
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PDB format | ![]() | 77 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5fgpC ![]() 3n8bS 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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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 9698.516 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37.87 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop Details: 50 mM MES pH 6.5, 200 mM NaCl, 16% PEG 3350 and 6 % MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 9, 2013 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9334 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. obs: 13999 / % possible obs: 96.5 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 19.4 |
Reflection shell | Resolution: 2.6→2.65 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 1.97 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3N8B Resolution: 2.6→47.725 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.12 / Phase error: 28.3 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→47.725 Å
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Refine LS restraints |
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LS refinement shell |
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