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Yorodumi- PDB-1axd: STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1axd | |||||||||
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Title | STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE | |||||||||
Components |
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Keywords | TRANSFERASE/TRANSFERASE INHIBITOR / TRANSFERASE / HERBICIDE DETOXIFICATION / TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX | |||||||||
Function / homology | Function and homology information response to salicylic acid / glutathione binding / response to herbicide / glutathione transferase / glutathione transferase activity / glutathione metabolic process / response to reactive oxygen species / response to hydrogen peroxide / response to xenobiotic stimulus / protein-containing complex / cytoplasm Similarity search - Function | |||||||||
Biological species | Zea mays (maize) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | |||||||||
Authors | Neuefeind, T. / Huber, R. / Dasenbrock, H. / Prade, L. / Bieseler, B. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism. Authors: Neuefeind, T. / Huber, R. / Dasenbrock, H. / Prade, L. / Bieseler, B. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1axd.cif.gz | 118.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1axd.ent.gz | 92.3 KB | Display | PDB format |
PDBx/mmJSON format | 1axd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ax/1axd ftp://data.pdbj.org/pub/pdb/validation_reports/ax/1axd | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 23330.891 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zea mays (maize) / Variant: MUTIN / Plasmid: PET3A / Production host: Escherichia coli (E. coli) / References: UniProt: P12653, glutathione transferase #2: Protein/peptide | Mass: 379.387 Da / Num. of mol.: 2 / Source method: isolated from a natural source #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.1 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 13788 / % possible obs: 92 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.089 |
Reflection | *PLUS Highest resolution: 2.5 Å |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å /
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Displacement parameters | Biso mean: 31.14 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.216 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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