+Open data
-Basic information
Entry | Database: PDB / ID: 7za4 | |||||||||
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Title | GSTF sh155 mutant | |||||||||
Components | Glutathione transferaseGlutathione S-transferase | |||||||||
Keywords | TRANSFERASE / Glutathione / Detoxification / Xenobiotics / Herbicides | |||||||||
Function / homology | Function and homology information response to chemical / glutathione transferase / glutathione transferase activity Similarity search - Function | |||||||||
Biological species | Alopecurus myosuroides (plant) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å | |||||||||
Authors | Papageorgiou, A.C. | |||||||||
Funding support | European Union, 2items
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Citation | Journal: Int J Mol Sci / Year: 2022 Title: Directed Evolution of Phi Class Glutathione Transferases Involved in Multiple-Herbicide Resistance of Grass Weeds and Crops. Authors: Ioannou, E. / Papageorgiou, A.C. / Labrou, N.E. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7za4.cif.gz | 168.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7za4.ent.gz | 108 KB | Display | PDB format |
PDBx/mmJSON format | 7za4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/za/7za4 ftp://data.pdbj.org/pub/pdb/validation_reports/za/7za4 | HTTPS FTP |
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-Related structure data
Related structure data | 7za5C 6rivS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25723.641 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: Missing residues because of high flexibility and no electron density. Source: (gene. exp.) Alopecurus myosuroides (plant) / Gene: GST2c / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9ZS17, glutathione transferase #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
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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: 2.28 Å3/Da / Density % sol: 46.03 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.8 / Details: Ammonium sulphate 0.2 M, PEG 4000 15-17.5% w/v |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 0.9918 Å |
Detector | Type: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Apr 9, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9918 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→83.1 Å / Num. obs: 43427 / % possible obs: 99 % / Redundancy: 4.9 % / Biso Wilson estimate: 39.97 Å2 / CC1/2: 0.998 / Rrim(I) all: 0.118 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.05→2.11 Å / Redundancy: 4.9 % / Mean I/σ(I) obs: 1 / Num. unique obs: 16765 / CC1/2: 0.456 / Rrim(I) all: 2.255 / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6riv Resolution: 2.05→45.31 Å / SU ML: 0.3009 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 32.2974 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.46 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.05→45.31 Å
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Refine LS restraints |
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LS refinement shell |
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