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Yorodumi- PDB-1xwk: 2.3 angstrom resolution crystal structure of human glutathione S-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xwk | ||||||
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Title | 2.3 angstrom resolution crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-S-dinitrobenzene | ||||||
Components | Glutathione S-transferase Mu 1 | ||||||
Keywords | TRANSFERASE / GLUTATHIONE / CONJUGATION / DETOXIFICATION / CYTOSOLIC / DIMER / ACTIVE SITE / GLUTATHIONYL-S-DINITROBENZENE / GS-DNB / 1-CHLORO-2 / 4-DINITROBENZENE / CDNB | ||||||
Function / homology | Function and homology information nitrobenzene metabolic process / cellular detoxification of nitrogen compound / glutathione derivative biosynthetic process / glutathione binding / hepoxilin biosynthetic process / Glutathione conjugation / Paracetamol ADME / Azathioprine ADME / prostaglandin metabolic process / intercellular bridge ...nitrobenzene metabolic process / cellular detoxification of nitrogen compound / glutathione derivative biosynthetic process / glutathione binding / hepoxilin biosynthetic process / Glutathione conjugation / Paracetamol ADME / Azathioprine ADME / prostaglandin metabolic process / intercellular bridge / glutathione transferase / glutathione transferase activity / xenobiotic catabolic process / glutathione metabolic process / enzyme binding / protein homodimerization activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Patskovsky, Y. / Patskovska, L. / Almo, S.C. / Listowsky, I. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a. Authors: Patskovsky, Y. / Patskovska, L. / Almo, S.C. / Listowsky, I. #1: Journal: Biochemistry / Year: 1999 Title: Functions of His-107 in the Catalytic Mechanism of Human Glutathione S-Transferase Hgstm1A-1A Authors: Patskovsky, Y.V. / Patskovska, L.N. / Listowsky, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xwk.cif.gz | 149.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xwk.ent.gz | 119.4 KB | Display | PDB format |
PDBx/mmJSON format | 1xwk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xwk_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 1xwk_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 1xwk_validation.xml.gz | 27.4 KB | Display | |
Data in CIF | 1xwk_validation.cif.gz | 37.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xw/1xwk ftp://data.pdbj.org/pub/pdb/validation_reports/xw/1xwk | HTTPS FTP |
-Related structure data
Related structure data | 1xw6C 2f3mC 1gtuS 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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2 |
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Unit cell |
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Details | The biological assembly is a dimer. The asymmetric unit contains three monomers, monomers A and C represent the homodimer, the second dimer can be generated from the monomer B by the operations : -x, y -z. |
-Components
#1: Protein | Mass: 25746.842 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GSTM1, GST1 / Plasmid: pET3a_hGSTM1a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P09488, glutathione transferase #2: Chemical | #3: 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: 2.35 Å3/Da / Density % sol: 47.3 % |
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Crystal grow | Temperature: 280 K / Method: vapor diffusion / pH: 6 Details: 20% PEG4000, pH 6.00, VAPOR DIFFUSION, temperature 280K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Mar 24, 2001 / Details: MIRRORS |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. all: 32953 / Num. obs: 27431 / % possible obs: 83.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 15.4 % / Biso Wilson estimate: 17.1 Å2 / Rmerge(I) obs: 0.06 / Rsym value: 0.051 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.269 / Mean I/σ(I) obs: 2.3 / Num. unique all: 1528 / Rsym value: 0.302 / % possible all: 47.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GTU Resolution: 2.3→20 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 100000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 21.6304 Å2 / ksol: 0.27122 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.048 / Total num. of bins used: 6
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Xplor file |
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