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Yorodumi- PDB-2cai: Structure of Glutathione-S-Transferase mutant, R21L, from Schisto... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2cai | ||||||
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Title | Structure of Glutathione-S-Transferase mutant, R21L, from Schistosoma Haematobium | ||||||
Components | GLUTATHIONE S-TRANSFERASE 28 KDA | ||||||
Keywords | TRANSFERASE / GLUTATHIONE S-TRANSFERASE / HOMODIMER / THIOREDOXIN-LIKE FOLD / DETOXIFICATION / ANTIGEN / MULTIGENE FAMILY | ||||||
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: 2.26 Å | ||||||
Authors | Baiocco, P. / Gourlay, L.J. / Angelucci, F. / Bellelli, A. / Brunori, M. / Miele, A.E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Probing the Mechanism of Gsh Activation in Schistosoma Haematobium Glutathione-S-Transferase by Site-Directed Mutagenesis and X-Ray Crystallography. Authors: Baiocco, P. / Gourlay, L.J. / Angelucci, F. / Fontaine, J. / Herve, M. / Miele, A.E. / Trottein, F. / Brunori, M. / Bellelli, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2cai.cif.gz | 102.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2cai.ent.gz | 80.3 KB | Display | PDB format |
PDBx/mmJSON format | 2cai.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2cai_validation.pdf.gz | 472.1 KB | Display | wwPDB validaton report |
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Full document | 2cai_full_validation.pdf.gz | 485.6 KB | Display | |
Data in XML | 2cai_validation.xml.gz | 21.6 KB | Display | |
Data in CIF | 2cai_validation.cif.gz | 29.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ca/2cai ftp://data.pdbj.org/pub/pdb/validation_reports/ca/2cai | HTTPS FTP |
-Related structure data
Related structure data | 2c80C 2c8uC 2ca8C 2caqC 2f8fC 1oe7S 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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-Components
#1: Protein | Mass: 23892.709 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) SCHISTOSOMA HAEMATOBIUM (invertebrata) / Plasmid: PET-23D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P30113, glutathione transferase #2: Chemical | ChemComp-SO4 / #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | IMPORTANT ROLE IN THE PARASITE DETOXIFICATION SYSTEM ENGINEERED RESIDUE IN CHAIN A, ARG 21 TO LEU ...IMPORTANT ROLE IN THE PARASITE DETOXIFICA | |
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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: 2.68 Å3/Da / Density % sol: 53.83 % |
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Crystal grow | pH: 7.4 Details: 10% PEG200, PBS PH7.4, 5MM MERCAPTOETHANOL, pH 7.40 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 14, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.26→20 Å / Num. obs: 25780 / % possible obs: 99.1 % / Observed criterion σ(I): 1 / Redundancy: 22 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 2.26→2.3 Å / Redundancy: 20.8 % / Mean I/σ(I) obs: 9.8 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1OE7 Resolution: 2.26→105.41 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.907 / SU B: 6.793 / SU ML: 0.172 / Cross valid method: THROUGHOUT / ESU R: 0.3 / ESU R Free: 0.241 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.25 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.26→105.41 Å
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Refine LS restraints |
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