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- PDB-1gul: HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gul | |||||||||
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Title | HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE | |||||||||
![]() | Glutathione S-transferase A4 | |||||||||
![]() | TRANSFERASE/TRANSFERASE INHIBITOR / ![]() | |||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bruns, C.M. / Hubatsch, I. / Ridderstrom, M. / Mannervik, B. / Tainer, J.A. | |||||||||
![]() | ![]() Title: Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products Authors: Bruns, C.M. / Hubatsch, I. / Ridderstrom, M. / Mannervik, B. / Tainer, J.A. #1: ![]() Title: Human Glutathione Transferase A4-4: An Alpha Class Enzyme with High Catalytic Efficiency in the Conjugation of 4-Hydroxynonenal and Other Genotoxic Products of Lipid Peroxidation Authors: Hubatsch, I. / Ridderstrom, M. / Mannervik, B. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 359.7 KB | Display | ![]() |
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PDB format | ![]() | 295.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1gumC ![]() 1gseS 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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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 25738.094 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-IBG / #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 55 % | |||||||||||||||
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Crystal grow![]() | pH: 7 Details: CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 20% PEG 4000, 100 MM PH 7.0, THEN SOAKED IN 1MM IODOBENZYL GLUTATHIONE | |||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 17, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.7→160 Å / Num. obs: 75834 / % possible obs: 86 % / Observed criterion σ(I): -3 / Redundancy: 8.7 % / Rsym value: 0.11 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 3.5 / Rsym value: 0.41 / % possible all: 99.8 |
Reflection | *PLUS Lowest resolution: 9999 Å / Num. obs: 58800 / Rmerge(I) obs: 0.11 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1GSE Resolution: 2.7→160 Å / Isotropic thermal model: TNT BCORREL V1.0 / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: TNT PROTGEO
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Solvent computation | Solvent model: BABINET SCALING / Bsol: 565.9 Å2 / ksol: 1.02 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→160 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.25 / Rfactor Rfree![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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