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Open data
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Basic information
Entry | Database: PDB / ID: 1oe7 | ||||||
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Title | 28kDa glutathione S-transferase from Schistosoma haematobium | ||||||
![]() | GLUTATHIONE S-TRANSFERASE![]() | ||||||
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Function / homology | ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Johnson, K.A. / Angelucci, F. / Tsernoglou, D. | ||||||
![]() | ![]() Title: Crystal Structure of the 28 kDa Glutathione S-Transferase from Schistosoma Haematobium Authors: Johnson, K.A. / Angelucci, F. / Bellelli, A. / Herve, M. / Fontaine, J. / Tsernoglou, D. / Capron, A. / Trottein, F. / Brunori, M. #1: Journal: J.Exp.Med. / Year: 2001 Title: Role of the Parasite-Derived Prostaglandin D2 in the Inhibition of Epidermal Langerhans Cell Migration During Schistosomiasis Infections Authors: Angeli, V. / Faveeuw, C. / Roye, O. / Fontaine, J. / Teissier, E. / Capron, A. / Wolowczuk, L. / Capron, M. / Trottein, F. #2: Journal: J.Mol.Biol. / Year: 1992 Title: Crystallization and Preliminary Diffraction Studies of a Protective Cloned 28 kDa Glutathione S-Transferase from Schistosoma Mansoni Authors: Trottein, F. / Vaney, M.C. / Bachet, B. / Pierce, R.J. / Colloc'H, N. / Lecocq, J.P. / Capron, A. / Momon, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101 KB | Display | ![]() |
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PDB format | ![]() | 77.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1oe8C ![]() 1gtbS 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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.0737, -0.0003, 0.9973), Vector ![]() |
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Components
#1: Protein | ![]() Mass: 23936.746 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() #2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() Sequence details | SEQUENCE MAPPED AGAINST ITSELF PENDING SEQUENCE SUBMISSION TO SWISSPROT DATABASE FOR SCHISTOSOMA ...SEQUENCE MAPPED AGAINST ITSELF PENDING SEQUENCE SUBMISSION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion, hanging drop / pH: 8 Details: PROTEIN (~60MG/ML) WAS CRYSTALLIZED IN HANGING DROPS USING A WELL SOLUTION OF 2.1M AMMONIUM SULFATE, 100MM TRIS, PH7.2, 5MM BETA-MERCAPTOETHANOL, pH 8.00 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.81→25 Å / Num. obs: 39246 / % possible obs: 96.3 % / Redundancy: 6.5 % / Biso Wilson estimate: 32.9 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 21.5 |
Reflection shell | Resolution: 1.81→1.86 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 3.4 / % possible all: 72 |
Reflection | *PLUS Redundancy: 6.5 % / Rmerge(I) obs: 0.071 |
Reflection shell | *PLUS % possible obs: 72 % / Redundancy: 2.6 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 3.4 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1GTB Resolution: 1.8→20 Å / SU B: 3.62 / SU ML: 0.11 / Cross valid method: THROUGHOUT / ESU R: 0.17 / ESU R Free: 0.17
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refinement | *PLUS Num. reflection obs: 39246 / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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