+Open data
-Basic information
Entry | Database: PDB / ID: 1gsd | ||||||
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Title | GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM | ||||||
Components | GLUTATHIONE TRANSFERASE A1-1 | ||||||
Keywords | TRANSFERASE (GLUTATHIONE) | ||||||
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 / SYNCHROTRON / Resolution: 2.5 Å | ||||||
Authors | L'Hermite, G. / Sinning, I. / 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 | 1gsd.cif.gz | 176 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gsd.ent.gz | 142.6 KB | Display | PDB format |
PDBx/mmJSON format | 1gsd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gsd_validation.pdf.gz | 444.9 KB | Display | wwPDB validaton report |
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Full document | 1gsd_full_validation.pdf.gz | 457 KB | Display | |
Data in XML | 1gsd_validation.xml.gz | 33 KB | Display | |
Data in CIF | 1gsd_validation.cif.gz | 40.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gs/1gsd ftp://data.pdbj.org/pub/pdb/validation_reports/gs/1gsd | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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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 | ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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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 2 .. A 438 TRANSFORMS A CHAIN OF DIMER TO A CHAIN OF SECOND DIMER OF THE ASYMMETRIC UNIT M2 B 2 .. B 438 TRANSFORMS B CHAIN OF DIMER TO B CHAIN OF SECOND DIMER OF THE ASYMMETRIC UNIT M3 A 2 .. A 438 B 2 .. B 438 0.001 TRANSFORMS A CHAIN OF DIMER TO B CHAIN OF DIMER |
-Components
#1: Protein | Mass: 25538.924 Da / Num. of mol.: 4 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: Water | ChemComp-HOH / | |
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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: 49.05 % | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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 | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.92 Å |
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Detector | Type: MARRESEARCH / Date: Sep 15, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 31802 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Rmerge(I) obs: 0.107 |
Reflection | *PLUS Num. measured all: 72511 / Rmerge(I) obs: 0.107 |
-Processing
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Refinement | Resolution: 2.5→7.5 Å / σ(F): 0 Details: RESIDUE ARG 89 HAS BEEN MODELLED IN TWO CONFORMATIONS AS FOR THE HIGHER RESOLUTION GST A 1-1 STRUCTURE COMPLEXED WITH A GLUTATHIONE, ETHACRYNIC ACID CONJUGATE. THIS RESIDUE LIES AT THE DIMER ...Details: RESIDUE ARG 89 HAS BEEN MODELLED IN TWO CONFORMATIONS AS FOR THE HIGHER RESOLUTION GST A 1-1 STRUCTURE COMPLEXED WITH A GLUTATHIONE, ETHACRYNIC ACID CONJUGATE. THIS RESIDUE LIES AT THE DIMER INTERFACE CLOSE TO AN NCS COPY OF ITSELF.
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Displacement parameters | Biso mean: 26 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→7.5 Å
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Refine LS restraints |
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