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- PDB-4wf7: Crystal structures of trehalose synthase from Deinococcus radiodu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4wf7 | ||||||
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Title | Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis | ||||||
![]() | Trehalose synthase | ||||||
![]() | ISOMERASE / Trehalose synthase / Glycoside hydrolase family 13 / Tris complex | ||||||
Function / homology | ![]() maltose alpha-D-glucosyltransferase / maltose alpha-D-glucosyltransferase activity / carbohydrate metabolic process / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wang, Y.L. / Chow, S.Y. / Lin, Y.T. / Hsieh, Y.C. / Lee, G.C. / Liaw, S.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization. Authors: Wang, Y.L. / Chow, S.Y. / Lin, Y.T. / Hsieh, Y.C. / Lee, G.C. / Liaw, S.H. #1: Journal: J. Agric. Food Chem. / Year: 2007 Title: Role of the C-terminal domain of Thermus thermophilus trehalose synthase in the thermophilicity, thermostability, and efficient production of trehalose. Authors: Wang, J.H. / Tsai, M.Y. / Chen, J.J. / Lee, G.C. / Shaw, J.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 463.6 KB | Display | ![]() |
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PDB format | ![]() | 375.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 479.3 KB | Display | ![]() |
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Full document | ![]() | 496.3 KB | Display | |
Data in XML | ![]() | 85.8 KB | Display | |
Data in CIF | ![]() | 122.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4tvuSC 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 64944.820 Da / Num. of mol.: 4 / Fragment: UNP residues 2-552 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() References: UniProt: I3NX86, maltose alpha-D-glucosyltransferase #2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-TRS / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.72 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 11% PEG 4000, 0.2M sodium acetate trihydrate, 0.3M Tris-HCl (pH 8.5), 5% glycerol |
-Data collection
Diffraction | Mean temperature: 110 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 22, 2014 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.21→20 Å / Num. obs: 129348 / % possible obs: 99.9 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.151 / Rpim(I) all: 0.066 / Rrim(I) all: 0.165 / Χ2: 0.918 / Net I/av σ(I): 12.594 / Net I/σ(I): 5.3 / Num. measured all: 759037 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4TVU Resolution: 2.21→20 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.948 / SU B: 5.409 / SU ML: 0.133 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.234 / ESU R Free: 0.178 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 93.49 Å2 / Biso mean: 32.96 Å2 / Biso min: 8.9 Å2
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Refinement step | Cycle: final / Resolution: 2.21→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.21→2.267 Å / Total num. of bins used: 20
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