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- PDB-7bib: Crystal structure of human GSTA1-1 bound to the glutathione adduc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7bib | ||||||
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Title | Crystal structure of human GSTA1-1 bound to the glutathione adduct of hexyl-isothiocyanate | ||||||
![]() | Glutathione S-transferase A1 | ||||||
![]() | TRANSFERASE / Glutathione transferase / ligandin | ||||||
Function / homology | ![]() Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process ...Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process / glutathione transferase / glutathione transferase activity / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / epithelial cell differentiation / xenobiotic metabolic process / glutathione metabolic process / fatty acid binding / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schwartz, M. / Neiers, F. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Role of human salivary enzymes in bitter taste perception. Authors: Schwartz, M. / Brignot, H. / Feron, G. / Hummel, T. / Zhu, Y. / von Koskull, D. / Heydel, J.M. / Lirussi, F. / Canon, F. / Neiers, 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 | ![]() | 108.2 KB | Display | ![]() |
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PDB format | ![]() | 76 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 | ![]() | 17.9 KB | Display | |
Data in CIF | ![]() | 24.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7biaC ![]() 7bicC ![]() 6yawS 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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Unit cell |
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Components
#1: Protein | Mass: 25670.121 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P08263, glutathione transferase, Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases, Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.14 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: Tris-HCl 0.1M pH 7.5, PEG4000 18% |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 12, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 2.03→46.61 Å / Num. obs: 29753 / % possible obs: 98.1 % / Redundancy: 6.7 % / Biso Wilson estimate: 37.76 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.111 / Rpim(I) all: 0.047 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 2.03→2.08 Å / Rmerge(I) obs: 1.051 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 1684 / CC1/2: 0.653 / Rpim(I) all: 0.624 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6YAW Resolution: 2.03→41.8 Å / SU ML: 0.3198 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 31.8723 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.98 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.03→41.8 Å
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Refine LS restraints |
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LS refinement shell |
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