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Yorodumi- PDB-1oe8: 28kDa glutathione S-transferase from Schistosoma haematobium (glu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1oe8 | ||||||
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Title | 28kDa glutathione S-transferase from Schistosoma haematobium (glutathione saturated) | ||||||
Components | GLUTATHIONE S-TRANSFERASE | ||||||
Keywords | TRANSFERASE / SCHISTOSOMIASIS / DETOXIFYING ENZYME / PROSTAGLANDIN D2 SYNTHASE / VACCINE CANDIDATE | ||||||
Function / homology | Function and homology information glutathione transferase / glutathione transferase activity / glutathione metabolic process Similarity search - Function | ||||||
Biological species | SCHISTOSOMA HAEMATOBIUM (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Johnson, K.A. / Angelucci, F. / Tsernoglou, D. | ||||||
Citation | Journal: Biochemistry / Year: 2003 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oe8.cif.gz | 104.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oe8.ent.gz | 79.7 KB | Display | PDB format |
PDBx/mmJSON format | 1oe8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1oe8_validation.pdf.gz | 952.1 KB | Display | wwPDB validaton report |
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Full document | 1oe8_full_validation.pdf.gz | 978.6 KB | Display | |
Data in XML | 1oe8_validation.xml.gz | 25 KB | Display | |
Data in CIF | 1oe8_validation.cif.gz | 34.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oe/1oe8 ftp://data.pdbj.org/pub/pdb/validation_reports/oe/1oe8 | HTTPS FTP |
-Related structure data
Related structure data | 1oe7C 1gtbS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-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: (-0.0596, -0.0001, 0.9982), Vector: |
-Components
#1: Protein | Mass: 23936.746 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SCHISTOSOMA HAEMATOBIUM (invertebrata) / Plasmid: PET-24D(+) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P30114*PLUS, glutathione transferase #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: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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) WITH 500UM EXCESS OF GSH 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: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A / Wavelength: 0.8431 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8431 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→25 Å / Num. obs: 51735 / % possible obs: 99.2 % / Redundancy: 4.1 % / Biso Wilson estimate: 28.5 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 40.9 |
Reflection shell | Resolution: 1.65→1.71 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2.7 / % possible all: 95 |
Reflection | *PLUS Redundancy: 4.1 % / Rmerge(I) obs: 0.04 |
Reflection shell | *PLUS % possible obs: 95 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GTB Resolution: 1.65→25 Å / SU B: 2.85 / SU ML: 0.1 / Cross valid method: THROUGHOUT / ESU R: 0.13 / ESU R Free: 0.13
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Refinement step | Cycle: LAST / Resolution: 1.65→25 Å
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Refinement | *PLUS Num. reflection obs: 51735 / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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