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- PDB-4grt: HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4grt | ||||||
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Title | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME | ||||||
![]() | GLUTATHIONE REDUCTASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stoll, V.S. / Simpson, S.J. / Krauth-Siegel, R.L. / Walsh, C.T. / Pai, E.F. | ||||||
![]() | ![]() Title: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Authors: Stoll, V.S. / Simpson, S.J. / Krauth-Siegel, R.L. / Walsh, C.T. / Pai, E.F. #1: ![]() Title: Redox Enzyme Engineering: Conversion of Human Glutathione Reductase Into a Trypanothione Reductase Authors: Bradley, M. / Bucheler, U.S. / Walsh, C.T. #2: ![]() Title: Refined Structure of Glutathione Reductase at 1.54 A Resolution Authors: Karplus, P.A. / Schulz, G.E. #3: ![]() Title: The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates Authors: Pai, E.F. / Schulz, G.E. #4: ![]() Title: Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase Authors: Wierenga, R.K. / Drenth, J. / Schulz, G.E. #5: ![]() Title: Glutathione Reductase from Human Erythrocytes. The Sequences of the Nadph Domain and of the Interface Domain Authors: Krauth-Siegel, R.L. / Blatterspiel, R. / Saleh, M. / Schiltz, E. / Schirmer, R.H. / Untucht-Grau, R. #6: ![]() Title: Fad-Binding Site of Glutathione Reductase Authors: Schulz, G.E. / Schirmer, R.H. / Pai, E.F. #7: ![]() Title: Three-Dimensional Structure of Glutathione Reductase at 2 A Resolution Authors: Thieme, R. / Pai, E.F. / Schirmer, R.H. / Schulz, G.E. #8: ![]() Title: Gene Duplication in Glutathione Reductase Authors: Schulz, G.E. #9: ![]() Title: The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine Authors: Untucht-Grau, R. / Schulz, G.E. / Schirmer, R.H. #10: ![]() Title: The Structure of the Flavoenzyme Glutathione Reductase Authors: Schulz, G.E. / Schirmer, R.H. / Sachsenheimer, W. / Pai, E.F. #11: ![]() Title: Low Resolution Structure of Human Erythrocyte Glutathione Reductase Authors: Zappe, H.A. / Krohne-Ehrich, G. / Schulz, G.E. #12: ![]() Title: Crystals of Human Erythrocyte Glutathione Reductase Authors: Schulz, G.E. / Zappe, H. / Worthington, D.J. / Rosemeyer, M.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 97.5 KB | Display | ![]() |
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PDB format | ![]() | 77.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1grtSC ![]() 2grtC ![]() 3grtC ![]() 5grtC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 50065.480 Da / Num. of mol.: 1 / Mutation: A34E, R37W Source method: isolated from a genetically manipulated source Details: CONTAINS A NON-COVALENTLY BOUND FAD AND OXIDIZED GLUTATHIONE SUBSTRATE Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FAD / ![]() |
#3: Chemical | ChemComp-GCG / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.99 % | ||||||||||||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion, hanging drop / pH: 8 Details: 0.57-0.90 M AMMONIUM SULFATE,100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION. CRYSTALS WERE SOAKED IN ARTIFICIAL MOTHER LIQUOR AT ...Details: 0.57-0.90 M AMMONIUM SULFATE,100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION. CRYSTALS WERE SOAKED IN ARTIFICIAL MOTHER LIQUOR AT PH 6.5 CONTAINING 420 MM OXIDIZED GLUTATHIONE, vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: May 1, 1993 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Highest resolution: 2.8 Å / Num. obs: 12974 / % possible obs: 86.6 % / Observed criterion σ(I): 0.1 / Redundancy: 1.5 % / Rsym value: 0.105 |
Reflection shell | Resolution: 2.8→2.93 Å / % possible all: 38.4 |
Reflection | *PLUS Num. obs: 12975 / Num. measured all: 19274 / Rmerge(I) obs: 0.105 |
Reflection shell | *PLUS % possible obs: 38.4 % |
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Processing
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Refinement | Method to determine structure![]() Starting model: PDB ENTRY 1GRT Resolution: 2.8→10 Å / Data cutoff high absF: 10000000 / σ(F): 0.1 Details: THE 17 N-TERMINAL AMINO ACIDS WERE DISORDERED AND NOT INCLUDED IN THE MODEL. THE MIXED DISULFIDE BETWEEN TRYPANOTHIONE IS A TRUE REACTION INTERMEDIATE.
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Refine analyze | Luzzati d res low obs: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.93 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 10245 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.1947 |