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Open data
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Basic information
Entry | Database: PDB / ID: 5lcz | ||||||
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Title | Chimeric GST | ||||||
![]() | Glutathione S-transferase A1,Glutathione S-transferase alpha-2,Glutathione S-transferase A1,Glutathione S-transferase alpha-2,Glutathione S-transferase A1 | ||||||
![]() | TRANSFERASE / Directed evolution / Glutathione transferase A1-1 / protein stability | ||||||
Function / homology | ![]() Azathioprine ADME / Glutathione conjugation / response to stilbenoid / Heme degradation / Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / : / dinitrosyl-iron complex binding / glutathione derivative biosynthetic process / glutathione binding / steroid delta-isomerase activity ...Azathioprine ADME / Glutathione conjugation / response to stilbenoid / Heme degradation / Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / : / dinitrosyl-iron complex binding / glutathione derivative biosynthetic process / glutathione binding / steroid delta-isomerase activity / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process / glutathione transferase / glutathione transferase activity / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / xenobiotic catabolic process / epithelial cell differentiation / xenobiotic metabolic process / glutathione metabolic process / fatty acid binding / response to bacterium / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Axarli, A. / Muleta, A.W. / Chronopoulou, E.G. / Papageorgiou, A.C. / Labrou, N.E. | ||||||
![]() | ![]() Title: Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability. Authors: Axarli, I. / Muleta, A.W. / Chronopoulou, E.G. / Papageorgiou, A.C. / Labrou, N.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.9 KB | Display | ![]() |
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PDB format | ![]() | 73.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 718.7 KB | Display | ![]() |
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Full document | ![]() | 726.4 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 25.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ld0C ![]() 1pkwS 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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Unit cell |
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Components
#1: Protein | Mass: 25780.139 Da / Num. of mol.: 2 Fragment: UNP residues 1-54,UNP residues 54-65,UNP residues 66-85,UNP residues 86-213,UNP residues 214-222 Source method: isolated from a genetically manipulated source Details: Protein obtained after gene shuffling of human and rat GSTA1-1 Source: (gene. exp.) ![]() ![]() ![]() Gene: GSTA1, Gsta2 / Production host: ![]() ![]() References: UniProt: P08263, UniProt: P04903, glutathione transferase #2: Chemical | ChemComp-GSH / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.41 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.4 / Details: PEG 4000 20% (w/v), ammonium citrate 0.2 M, pH 6.4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 19, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8081 Å / Relative weight: 1 |
Reflection | Resolution: 2.32→20 Å / Num. obs: 19517 / % possible obs: 98.5 % / Redundancy: 4.2 % / Biso Wilson estimate: 51.4 Å2 / CC1/2: 0.992 / Rsym value: 0.0112 / Net I/σ(I): 9.04 |
Reflection shell | Resolution: 2.32→2.39 Å / Rmerge(I) obs: 0.509 / Mean I/σ(I) obs: 2.3 / % possible all: 83.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1pkw Resolution: 2.325→19.669 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 31.64 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.325→19.669 Å
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Refine LS restraints |
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LS refinement shell |
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