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- PDB-5u56: Structure of Francisella tularensis heterodimeric SspA (MglA-SspA) -
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Open data
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Basic information
Entry | Database: PDB / ID: 5u56 | ||||||
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Title | Structure of Francisella tularensis heterodimeric SspA (MglA-SspA) | ||||||
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![]() | TRANSCRIPTION / Stringent starvation protein A / Macrophage growth locus A / GST-fold | ||||||
Function / homology | ![]() glutathione dehydrogenase (ascorbate) activity / L-ascorbic acid metabolic process / glutathione transferase activity / glutathione metabolic process / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cuthbert, B.J. / Schumacher, M.A. / Brennan, R.G. | ||||||
![]() | ![]() Title: Dissection of the molecular circuitry controlling virulence in Francisella tularensis. Authors: Cuthbert, B.J. / Ross, W. / Rohlfing, A.E. / Dove, S.L. / Gourse, R.L. / Brennan, R.G. / Schumacher, M.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 171.1 KB | Display | ![]() |
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PDB format | ![]() | 133.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 493 KB | Display | ![]() |
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Full document | ![]() | 500.5 KB | Display | |
Data in XML | ![]() | 30.5 KB | Display | |
Data in CIF | ![]() | 40.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5u51C ![]() 6alxC ![]() 1yy7S ![]() 4purS 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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Unit cell |
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Components
-Protein , 2 types, 4 molecules CDAB
#1: Protein | Mass: 24110.094 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 23594.529 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Details (production host): Expressed as an MBP fusion protein from pMCSG9 Cell line (production host): C41 (DE3) / Production host: ![]() ![]() |
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-Non-polymers , 4 types, 76 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PRO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/1PE.gif)
![](data/chem/img/PRO.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-GOL / #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.55 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: PEGRX2 17 L-proline, HEPES, PEG 1500 |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 15, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9774 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→50 Å / Num. obs: 31478 / % possible obs: 99.9 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 31.74 |
Reflection shell | Resolution: 2.65→2.7 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.784 / Mean I/σ(I) obs: 2.13 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4PUR, 1YY7 Resolution: 2.65→44.077 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.32 / 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: 2.65→44.077 Å
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Refine LS restraints |
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LS refinement shell |
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