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- PDB-1n2a: Crystal Structure of a Bacterial Glutathione Transferase from Esc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n2a | ||||||
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Title | Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site | ||||||
![]() | Glutathione S-transferase | ||||||
![]() | TRANSFERASE | ||||||
Function / homology | ![]() glutathione transferase / glutathione transferase activity / response to hydrogen peroxide / protein homodimerization activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Rife, C.L. / Parsons, J.F. / Xiao, G. / Gilliland, G.L. / Armstrong, R.N. | ||||||
![]() | ![]() Title: Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli Authors: Rife, C.L. / Parsons, J.F. / Xiao, G. / Gilliland, G.L. / Armstrong, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92.8 KB | Display | ![]() |
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PDB format | ![]() | 71.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 964.4 KB | Display | ![]() |
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Full document | ![]() | 978.2 KB | Display | |
Data in XML | ![]() | 19.7 KB | Display | |
Data in CIF | ![]() | 26.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1aofS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | The biological assembly is a dimer composed of chains A and B. |
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Components
#1: Protein | Mass: 22896.342 Da / Num. of mol.: 2 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: 2 Å3/Da / Density % sol: 38.63 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.7 Details: PEG 3000, B-n-octyl-glucopyranoside, glutathione sulfonate, sodium acetate, pH 4.7, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 10, 1997 |
Radiation | Monochromator: Yale mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→19.7 Å / Num. obs: 23318 / % possible obs: 87.53 % / Observed criterion σ(F): 4 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.042 |
Reflection | *PLUS % possible obs: 86.8 % / Redundancy: 11 % / Rmerge(I) obs: 0.041 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 1.97 Å / % possible obs: 41.6 % / Rmerge(I) obs: 0.22 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1AOF Resolution: 1.9→19.17 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.901 / SU B: 4.128 / SU ML: 0.121 / Cross valid method: THROUGHOUT / σ(F): 4 / ESU R: 0.229 / ESU R Free: 0.202 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.321 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→19.17 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.953 Å / Total num. of bins used: 20
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Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 19.7 Å / Num. reflection obs: 21775 / Rfactor Rfree: 0.26 / Rfactor Rwork: 0.194 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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