+Open data
-Basic information
Entry | Database: PDB / ID: 3crt | ||||||
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Title | Structural characterization of an engineered allosteric protein | ||||||
Components | Glutathione S-transferase class-mu 26 kDa isozyme | ||||||
Keywords | TRANSFERASE / protein design / engineered allostery. pH-switch | ||||||
Function / homology | Function and homology information glutathione transferase / glutathione transferase activity / glutathione metabolic process Similarity search - Function | ||||||
Biological species | Schistosoma japonicum (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Sagermann, M. / Chapleau, R. / DeLorimier, E. / Lei, M. | ||||||
Citation | Journal: Protein Sci. / Year: 2009 Title: Using affinity chromatography to engineer and characterize pH-dependent protein switches. Authors: Sagermann, M. / Chapleau, R.R. / DeLorimier, E. / Lei, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3crt.cif.gz | 60.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3crt.ent.gz | 43.7 KB | Display | PDB format |
PDBx/mmJSON format | 3crt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3crt_validation.pdf.gz | 736.4 KB | Display | wwPDB validaton report |
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Full document | 3crt_full_validation.pdf.gz | 745.9 KB | Display | |
Data in XML | 3crt_validation.xml.gz | 13.6 KB | Display | |
Data in CIF | 3crt_validation.cif.gz | 18.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cr/3crt ftp://data.pdbj.org/pub/pdb/validation_reports/cr/3crt | HTTPS FTP |
-Related structure data
Related structure data | 3cruC 3d0zC 1gneS 3crs S: Starting model for refinement C: citing same article (ref.) |
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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: 25063.148 Da / Num. of mol.: 1 / Mutation: L50C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schistosoma japonicum (invertebrata) / Gene: GST / Plasmid: pET151 / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21-AI / References: UniProt: P08515, glutathione transferase |
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#2: Chemical | ChemComp-GSH / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.97 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 20% PEG8000, 50mM tris, 5mM B-mercaptoethanol , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 150 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR-H / Wavelength: 1.5418 Å |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Jun 5, 2007 / Details: Helios optics |
Radiation | Monochromator: Bruker Helios optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→19.5 Å / Num. all: 36529 / Num. obs: 34548 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.85 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 20.56 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDBID: 1GNE Resolution: 1.9→19.5 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: last residues HPPK could not be modeled reliably into the electron density map.
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.9→19.5 Å
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Refine LS restraints |
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