+Open data
-Basic information
Entry | Database: PDB / ID: 1k3o | ||||||
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Title | Crystal Structure Analysis of apo Glutathione S-Transferase | ||||||
Components | GLUTATHIONE S-TRANSFERASE A1 | ||||||
Keywords | TRANSFERASE / apo glutatione S-transferase | ||||||
Function / homology | Function and homology information Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process ...Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process / glutathione transferase / glutathione transferase activity / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / epithelial cell differentiation / xenobiotic metabolic process / glutathione metabolic process / fatty acid binding / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Le Trong, I. / Stenkamp, R.E. / Ibarra, C. / Atkins, W.M. / Adman, E.T. | ||||||
Citation | Journal: Proteins / Year: 2002 Title: 1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site. Authors: Le Trong, I. / Stenkamp, R.E. / Ibarra, C. / Atkins, W.M. / Adman, E.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1k3o.cif.gz | 98.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1k3o.ent.gz | 75.1 KB | Display | PDB format |
PDBx/mmJSON format | 1k3o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1k3o_validation.pdf.gz | 424.1 KB | Display | wwPDB validaton report |
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Full document | 1k3o_full_validation.pdf.gz | 432.1 KB | Display | |
Data in XML | 1k3o_validation.xml.gz | 19.8 KB | Display | |
Data in CIF | 1k3o_validation.cif.gz | 28.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k3/1k3o ftp://data.pdbj.org/pub/pdb/validation_reports/k3/1k3o | HTTPS FTP |
-Related structure data
Related structure data | 1k3lC 1k3yC 1gseS 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 25538.924 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P08263, glutathione transferase #2: Water | ChemComp-HOH / | |
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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: 2.4 Å3/Da / Density % sol: 48.8 % |
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Crystal grow | Method: vapor diffusion, sitting drop / pH: 7.5 Details: 22% PEG3350, 0.1M Tris-Cl 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 100K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.98 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 27, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. all: 48158 / Num. obs: 43692 / % possible obs: 90.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.055 |
Reflection shell | Resolution: 1.8→1.83 Å / Rmerge(I) obs: 0.292 / Num. unique all: 874 / % possible all: 36.5 |
-Processing
Software |
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Refinement | Starting model: PDB ENTRY 1GSE [NO WATER OR LIGAND] Resolution: 1.8→10 Å / Num. parameters: 14173 / Num. restraintsaints: 10093 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Refine analyze | Num. disordered residues: 3 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 3513.5 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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