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- PDB-2c4j: Human glutathione-S-transferase M2-2 T210S mutant in complex with... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2c4j | ||||||
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Title | Human glutathione-S-transferase M2-2 T210S mutant in complex with glutathione-styrene oxide conjugate | ||||||
![]() | GLUTATHIONE S-TRANSFERASE MU 2 | ||||||
![]() | TRANSFERASE / GLUTATHIONE / GLUTATHIONE TRANSFERASE / M2-2 / MULTIGENE FAMILY | ||||||
Function / homology | ![]() nitrobenzene metabolic process / cellular detoxification of nitrogen compound / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / relaxation of cardiac muscle / intercellular bridge ...nitrobenzene metabolic process / cellular detoxification of nitrogen compound / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / relaxation of cardiac muscle / intercellular bridge / positive regulation of ryanodine-sensitive calcium-release channel activity / cellular response to caffeine / glutathione transferase / glutathione transferase activity / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / xenobiotic catabolic process / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / glutathione metabolic process / sarcoplasmic reticulum / fatty acid binding / signaling receptor binding / enzyme binding / protein homodimerization activity / extracellular exosome / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tars, K. / Andersson, M. / Ivarsson, Y. / Olin, B. / Mannervik, B. | ||||||
![]() | ![]() Title: Alternative Mutations of a Positively Selected Residue Elicit Gain or Loss of Functionalities in Enzyme Evolution. Authors: Norrgard, M.A. / Ivarsson, Y. / Tars, K. / 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 | ![]() | 210.2 KB | Display | ![]() |
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PDB format | ![]() | 169.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 42.8 KB | Display | |
Data in CIF | ![]() | 64.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2gtuS 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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1 | ![]()
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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: 25762.627 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-GSO / #3: Water | ChemComp-HOH / | Compound details | CONJUGATES REDUCED GLUTATHIONE TO A LARGE NUMBER OF EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ...CONJUGATES | Sequence details | RESIDUE THR 210 IS MUTATED TO SERINE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 39.92 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 8 Details: HANGING DROP VAPOUR TECHNIQUE. 5 MICRLITRES OF PROTEIN AT 10MG/ML IN 20 MM TRIS-HCL, PH 8.0 WERE MIXED WITH 5 MICROLITRES OF RESERVOIR SOLUTION CONTAINING 100 MM TRIS-HCL, PH 7.8, 2MM DTT, ...Details: HANGING DROP VAPOUR TECHNIQUE. 5 MICRLITRES OF PROTEIN AT 10MG/ML IN 20 MM TRIS-HCL, PH 8.0 WERE MIXED WITH 5 MICROLITRES OF RESERVOIR SOLUTION CONTAINING 100 MM TRIS-HCL, PH 7.8, 2MM DTT, 25% PEG 4000 AND 1 MICROLITRE OF 20MM GLUTATHIONE CONJUGATE WITH STYRENE OXIDE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 21, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→30 Å / Num. obs: 194076 / % possible obs: 98.2 % / Observed criterion σ(I): 2.8 / Redundancy: 3.2 % / Biso Wilson estimate: 14.05 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 23 |
Reflection shell | Resolution: 1.35→1.37 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.85 / Mean I/σ(I) obs: 2.8 / % possible all: 87.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2GTU Resolution: 1.35→30 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.955 / SU B: 1.032 / SU ML: 0.042 / Cross valid method: THROUGHOUT / ESU R: 0.061 / ESU R Free: 0.061 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 18.63 Å2
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Refinement step | Cycle: LAST / Resolution: 1.35→30 Å
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Refine LS restraints |
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