+Open data
-Basic information
Entry | Database: PDB / ID: 2caq | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of R21L mutant of Sh28GST in complex with GSH | ||||||
Components | GLUTATHIONE S-TRANSFERASE 28 KDA | ||||||
Keywords | TRANSFERASE / SIGMA CLASS GST / DETOXIFICATION / GLUTATHIONE / PROSTAGLANDIN D2 SYNTHASE / ANTIGEN | ||||||
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 Å | ||||||
Authors | Baiocco, P. / Gourlay, L.J. / Angelucci, F. / Bellelli, A. / Miele, A.E. / Brunori, M. | ||||||
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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2caq.cif.gz | 63.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2caq.ent.gz | 45.3 KB | Display | PDB format |
PDBx/mmJSON format | 2caq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2caq_validation.pdf.gz | 737.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2caq_full_validation.pdf.gz | 743 KB | Display | |
Data in XML | 2caq_validation.xml.gz | 13.9 KB | Display | |
Data in CIF | 2caq_validation.cif.gz | 19.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ca/2caq ftp://data.pdbj.org/pub/pdb/validation_reports/ca/2caq | HTTPS FTP |
-Related structure data
Related structure data | 2c80C 2c8uC 2ca8C 2caiC 2f8fC 1oe7S C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-Components
#1: Protein | Mass: 23892.709 Da / Num. of mol.: 1 / 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-GSH / |
#3: Chemical | ChemComp-PG4 / |
#4: Chemical | ChemComp-BME / |
#5: Water | ChemComp-HOH / |
Compound details | INVOLVED IN THE CONJUGATION OF REDUCED GLUTATHIONE TO A LARGE NUMBER OF EXOGENOUS AND ENDOGENOUS ...INVOLVED IN THE CONJUGATIO |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.63 % |
---|---|
Crystal grow | pH: 6 Details: 2.3 M (NH4)2SO4 PBS PH 7.4 5 MM ETANTHIOL 10% PEG 200 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 0.931 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 21, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2→47.3 Å / Num. obs: 16536 / % possible obs: 98.4 % / Observed criterion σ(I): 1 / Redundancy: 5.6 % / Biso Wilson estimate: 23.67 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 19.9 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.13 / Mean I/σ(I) obs: 10.3 / % possible all: 98.7 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1OE7 Resolution: 2→47.3 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.911 / SU B: 3.776 / SU ML: 0.109 / Cross valid method: THROUGHOUT / ESU R: 0.192 / ESU R Free: 0.173 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 23.57 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→47.3 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|