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Yorodumi- PDB-1gse: GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gse | ||||||
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Title | GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K) | ||||||
Components | GLUTATHIONE TRANSFERASE | ||||||
Keywords | TRANSFERASE (GLUTATHIONE) / A1-1 | ||||||
Function / homology | Function and homology information Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process / glutathione transferase ...Isomerases; Intramolecular oxidoreductases; Transposing C=C bonds / glutathione derivative biosynthetic process / steroid delta-isomerase activity / Glutathione conjugation / glutathione peroxidase activity / Azathioprine ADME / Heme degradation / NFE2L2 regulating anti-oxidant/detoxification enzymes / prostaglandin metabolic process / glutathione transferase / glutathione transferase activity / epithelial cell differentiation / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / linoleic acid metabolic process / glutathione metabolic process / xenobiotic metabolic process / fatty acid binding / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Cameron, A.D. / Jones, T.A. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Authors: Cameron, A.D. / Sinning, I. / L'Hermite, G. / Olin, B. / Board, P.G. / Mannervik, B. / Jones, T.A. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Structure Determination and Refinement of Human Alpha Class Glutathione Transferase A1-1, and a Comparison with the Mu and Pi Class Enzyme Authors: Sinning, I. / Kleywegt, G.J. / Cowan, S.W. / Reinemer, P. / Dirr, H.W. / Huber, R. / Gilliland, G.L. / Armstrong, R.N. / Ji, X. / Board, P.G. / Olin, B. / Mannervik, B. / Jones, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gse.cif.gz | 113.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gse.ent.gz | 88.1 KB | Display | PDB format |
PDBx/mmJSON format | 1gse.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gse_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 1gse_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 1gse_validation.xml.gz | 24 KB | Display | |
Data in CIF | 1gse_validation.cif.gz | 33.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gs/1gse ftp://data.pdbj.org/pub/pdb/validation_reports/gs/1gse | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 56 / 2: CIS PROLINE - PRO B 56 | |||||||||||||||
Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.60546, 0.04633, 0.79453), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 4 .. A 222 B 4 .. B 222 0.123 | |
-Components
#1: Protein | Mass: 25510.910 Da / Num. of mol.: 2 / Mutation: R15K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: LIVER / Plasmid: PTACGST2 / Production host: Escherichia coli (E. coli) / Strain (production host): JM103 / References: UniProt: P08263, glutathione transferase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-BME / #5: Water | ChemComp-HOH / | Nonpolymer details | THE ETHACRYNIC ACID MOIETY OF THE LIGAND HAS BEEN MODELLED IN TWO ALTERNATE CONFORMATIONS. TO ...THE ETHACRYNIC | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.99 % | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jan 20, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. obs: 30538 / % possible obs: 93.4 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Rmerge(I) obs: 0.073 |
Reflection | *PLUS Num. measured all: 64609 / Rmerge(I) obs: 0.073 |
-Processing
Software |
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Refinement | Resolution: 2→7.5 Å / σ(F): 0 Details: TWO B-MERCAPTOETHANOL RESIDUES (SEO) HAVE BEEN INSERTED INTO EACH MONOMER SUCH THAT THEY FORM A 2-HYDROXYETHYL DISULFIDE (RESIDUES 225 AND 226). IN EACH CASE ONE OF THE BME'S HAS BEEN ...Details: TWO B-MERCAPTOETHANOL RESIDUES (SEO) HAVE BEEN INSERTED INTO EACH MONOMER SUCH THAT THEY FORM A 2-HYDROXYETHYL DISULFIDE (RESIDUES 225 AND 226). IN EACH CASE ONE OF THE BME'S HAS BEEN MODELLED IN TWO CONFORMATIONS.
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Displacement parameters | Biso mean: 27 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→7.5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.244 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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