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- PDB-1ev4: RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ev4 | ||||||
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Title | RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND | ||||||
![]() | GLUTATHIONE S-TRANSFERASE A1-1 | ||||||
![]() | TRANSFERASE / disordered C-terminal helices | ||||||
Function / homology | ![]() Azathioprine ADME / Glutathione conjugation / Heme degradation / Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / dinitrosyl-iron complex binding / glutathione derivative biosynthetic process / glutathione binding / steroid delta-isomerase activity / linoleic acid metabolic process / glutathione peroxidase activity ...Azathioprine ADME / Glutathione conjugation / Heme degradation / Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / dinitrosyl-iron complex binding / glutathione derivative biosynthetic process / glutathione binding / steroid delta-isomerase activity / linoleic acid metabolic process / glutathione peroxidase activity / prostaglandin metabolic process / glutathione transferase / glutathione transferase activity / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / xenobiotic catabolic process / epithelial cell differentiation / xenobiotic metabolic process / response to nutrient levels / glutathione metabolic process / fatty acid binding / response to xenobiotic stimulus / protein homodimerization activity / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Adman, E.T. / Le Trong, I. / Stenkamp, R.E. / Nieslanik, B.S. / Dietze, E.C. / Tai, G. / Ibarra, C. / Atkins, W.M. | ||||||
![]() | ![]() Title: Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y. Authors: Adman, E.T. / Le Trong, I. / Stenkamp, R.E. / Nieslanik, B.S. / Dietze, E.C. / Tai, G. / Ibarra, C. / Atkins, W.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 147.9 KB | Display | ![]() |
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PDB format | ![]() | 117.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 30.6 KB | Display | |
Data in CIF | ![]() | 42.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Details | chain A forms crystallographic dimer chains C&D form non-crystallographic dimer |
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Components
#1: Protein | Mass: 25480.885 Da / Num. of mol.: 3 / Mutation: W21F/F220Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.02 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.1M HEPES, 60% saturated ammonium sulfate, 1 mM S-hexyl glutathione , pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K | |||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Nov 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. all: 61093 / Num. obs: 58664 / % possible obs: 77 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.054 / Net I/σ(I): 14.6 |
Reflection shell | Resolution: 1.8→1.88 Å / Rmerge(I) obs: 0.3 / % possible all: 15.3 |
Reflection | *PLUS Highest resolution: 1.88 Å / % possible obs: 85 % / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS Highest resolution: 1.88 Å / Lowest resolution: 1.98 Å / % possible obs: 45 % / Num. unique obs: 4452 / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 2.3 |
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Processing
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Refinement | Resolution: 2.2→20 Å / σ(F): 5 / σ(I): 5 / Stereochemistry target values: Engh & Humber Details: XPLOR version 3.8 used bulk solvent correction (KSOL=0.8, BSOL = 20.) anisotropic overall B correction -3.0,2.2,0.84
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 19.8 Å / σ(F): 5 / % reflection Rfree: 10 % / Rfactor obs: 0.218 / Rfactor Rfree: 0.286 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 2.2 |