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Yorodumi- PDB-1ags: A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERAS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ags | ||||||
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Title | A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL | ||||||
Components | GLUTATHIONE S-TRANSFERASE ALPHA | ||||||
Keywords | TRANSFERASE (GLUTATHIONE) | ||||||
Function / homology | Function and homology information Glutathione conjugation / Azathioprine ADME / glutathione transferase / glutathione transferase activity / epithelial cell differentiation / glutathione metabolic process / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / xenobiotic metabolic process / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Zeng, K. / Rose, J.P. / Wang, B.C. | ||||||
Citation | Journal: Proteins / Year: 1994 Title: A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Authors: Zeng, K. / Rose, J.P. / Chen, H.C. / Strickland, C.L. / Tu, C.P. / Wang, B.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ags.cif.gz | 25.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ags.ent.gz | 13 KB | Display | PDB format |
PDBx/mmJSON format | 1ags.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ags_validation.pdf.gz | 365.1 KB | Display | wwPDB validaton report |
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Full document | 1ags_full_validation.pdf.gz | 365.1 KB | Display | |
Data in XML | 1ags_validation.xml.gz | 1.3 KB | Display | |
Data in CIF | 1ags_validation.cif.gz | 5.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ag/1ags ftp://data.pdbj.org/pub/pdb/validation_reports/ag/1ags | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25687.020 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Gene: PGTH121-G82R / Organ: LIVER / Plasmid: PKK223-3 / Gene (production host): PGTH121-G82R / Production host: Escherichia coli (E. coli) / References: UniProt: P09210, glutathione transferase #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.55 % | |||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 54 % | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 8 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 18098 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.0996 |
Reflection | *PLUS Highest resolution: 2.5 Å / % possible obs: 92.6 % / Rmerge(I) obs: 0.0996 |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | |||||||||||||||
Refinement | *PLUS | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS |