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Open data
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Basic information
Entry | Database: PDB / ID: 2c3n | ||||||
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Title | Human glutathione-S-transferase T1-1, apo form | ||||||
![]() | GLUTATHIONE S-TRANSFERASE THETA 1 | ||||||
![]() | TRANSFERASE / GLUTATHIONE / GLUTATHIONE TRANSFERASE / T1-1 / POLYMORPHISM | ||||||
Function / homology | ![]() Glutathione conjugation / Paracetamol ADME / glutathione peroxidase activity / glutathione transferase / glutathione transferase activity / glutathione metabolic process / extracellular exosome / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tars, K. / Larsson, A.-K. / Shokeer, A. / Olin, B. / Mannervik, B. / Kleywegt, G.J. | ||||||
![]() | ![]() Title: Structural Basis of the Suppressed Catalytic Activity of Wild-Type Human Glutathione Transferase T1-1 Compared to its W234R Mutant. Authors: Tars, K. / Larsson, A.-K. / Shokeer, A. / Olin, B. / Mannervik, B. / Kleywegt, G.J. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 212.4 KB | Display | ![]() |
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PDB format | ![]() | 171.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.1 KB | Display | ![]() |
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Full document | ![]() | 447.8 KB | Display | |
Data in XML | ![]() | 42.1 KB | Display | |
Data in CIF | ![]() | 61.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2c3qC ![]() 2c3tC ![]() 1ljrS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 28329.084 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-IOD / #3: Water | ChemComp-HOH / | Compound details | CONJUGATES | Sequence details | 6XHIS TAG ADDED TO THE N-TERMINUS OF PROTEIN | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.68 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 8 Details: HANGING DROP VAPOUR DIFFUSION TECHINQUE; 5 MICROLITRES OF RESERVOIR SOLUTION [35% (V/V) PEG 3350,200 MM MG(NO3)2, 200MM NAI, 2 MM DTT] WAS MIXED WITH 5 MICROLITRES OF PROTEIN SOLUTION (10 ...Details: HANGING DROP VAPOUR DIFFUSION TECHINQUE; 5 MICROLITRES OF RESERVOIR SOLUTION [35% (V/V) PEG 3350,200 MM MG(NO3)2, 200MM NAI, 2 MM DTT] WAS MIXED WITH 5 MICROLITRES OF PROTEIN SOLUTION (10 MG/ML IN 10 MM TRIS-HCL PH 7.8, 15 % GLYCEROL) AND 1 MICROLITRE OF 100 MM CACL2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 2, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.94 Å / Relative weight: 1 |
Reflection | Resolution: 1.51→30 Å / Num. obs: 161402 / % possible obs: 97.7 % / Observed criterion σ(I): 2.3 / Redundancy: 2.9 % / Biso Wilson estimate: 22 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 20.4 |
Reflection shell | Resolution: 1.51→1.54 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 2.3 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LJR Resolution: 1.5→30 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.943 / SU B: 1.584 / SU ML: 0.06 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.088 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE N-TERMINAL 6XHIS TAG AND THE FOLLOWING METHIONINE IS DISORDERED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.22 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→30 Å
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Refine LS restraints |
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