+Open data
-Basic information
Entry | Database: PDB / ID: 1gnw | ||||||
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Title | STRUCTURE OF GLUTATHIONE S-TRANSFERASE | ||||||
Components | GLUTATHIONE S-TRANSFERASE | ||||||
Keywords | TRANSFERASE / HERBICIDE DETOXIFICATION | ||||||
Function / homology | Function and homology information response to oomycetes / camalexin binding / quercitrin binding / salicylic acid binding / toxin catabolic process / auxin-activated signaling pathway / glutathione binding / plasmodesma / apoplast / plant-type vacuole ...response to oomycetes / camalexin binding / quercitrin binding / salicylic acid binding / toxin catabolic process / auxin-activated signaling pathway / glutathione binding / plasmodesma / apoplast / plant-type vacuole / chloroplast stroma / response to zinc ion / glutathione transferase / glutathione transferase activity / response to cadmium ion / response to cold / chloroplast / peroxidase activity / defense response / protein domain specific binding / intracellular membrane-bounded organelle / endoplasmic reticulum / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Reinemer, P. / Prade, L. / Hof, P. / Neuefeind, T. / Huber, R. / Palme, K. / Bartunik, H.D. / Bieseler, B. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases ...Title: Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. Authors: Reinemer, P. / Prade, L. / Hof, P. / Neuefeind, T. / Huber, R. / Zettl, R. / Palme, K. / Schell, J. / Koelln, I. / Bartunik, H.D. / Bieseler, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gnw.cif.gz | 124.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gnw.ent.gz | 99.5 KB | Display | PDB format |
PDBx/mmJSON format | 1gnw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gnw_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1gnw_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1gnw_validation.xml.gz | 21.3 KB | Display | |
Data in CIF | 1gnw_validation.cif.gz | 29.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gn/1gnw ftp://data.pdbj.org/pub/pdb/validation_reports/gn/1gnw | HTTPS FTP |
-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: 24031.371 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Plasmid: PET3A / Production host: Escherichia coli (E. coli) / References: UniProt: P46422, glutathione transferase #2: Chemical | ChemComp-GTX / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.38 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 23438 / % possible obs: 88.9 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.094 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 9999 Å |
Reflection shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.23 Å / % possible obs: 46.2 % |
-Processing
Software |
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Refinement | Resolution: 2.2→8 Å /
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Displacement parameters | Biso mean: 19.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.19 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.22 Å / Rfactor obs: 0.289 |