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- PDB-1gra: SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIV... -
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Basic information
Entry | Database: PDB / ID: 1gra | |||||||||
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Title | SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | |||||||||
![]() | GLUTATHIONE REDUCTASE | |||||||||
![]() | OXIDOREDUCTASE / OXIDOREDUCTASE(FLAVOENZYME) | |||||||||
Function / homology | ![]() glutathione-disulfide reductase / Metabolism of ingested H2SeO4 and H2SeO3 into H2Se / glutathione-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / NFE2L2 regulating anti-oxidant/detoxification enzymes / Detoxification of Reactive Oxygen Species / glutathione metabolic process / cell redox homeostasis / TP53 Regulates Metabolic Genes / NADP binding ...glutathione-disulfide reductase / Metabolism of ingested H2SeO4 and H2SeO3 into H2Se / glutathione-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / NFE2L2 regulating anti-oxidant/detoxification enzymes / Detoxification of Reactive Oxygen Species / glutathione metabolic process / cell redox homeostasis / TP53 Regulates Metabolic Genes / NADP binding / flavin adenine dinucleotide binding / cellular response to oxidative stress / electron transfer activity / mitochondrial matrix / external side of plasma membrane / mitochondrion / extracellular exosome / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Karplus, P.A. / Schulz, G.E. | |||||||||
![]() | ![]() Title: Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. Authors: Karplus, P.A. / Schulz, G.E. #1: ![]() Title: Inhibition of Human Glutathione Reductase by the Nitrosourea Drugs 1,3-Bis(2-Chloroethyl)-1-Nitrosourea and 1-(2-Chloroethyl)-3-(2-Hydroxyethyl)-1-Nitrosourea Authors: Karplus, P.A. / Krauth-Siegel, R.L. / Schirmer, R.H. / Schulz, G.E. #2: ![]() Title: Refined Structure of Glutathione Reductase at 1.54 Angstroms Resolution Authors: Karplus, P.A. / Schulz, G.E. #3: ![]() Title: Interaction of a Glutathione S-Conjugate with Glutathione Reductase. Kinetic and X-Ray Crystallographic Studies Authors: Bilzer, M. / Krauth-Siegel, R.L. / Schirmer, R.H. / Akerboom, T.P.M. / Sies, H. / 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: The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates Authors: Pai, E.F. / Schulz, G.E. #6: ![]() Title: Fad-Binding Site of Glutathione Reductase Authors: Schulz, G.E. / Schirmer, R.H. / Pai, E.F. #7: ![]() 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. #8: ![]() Title: Three-Dimensional Structure of Glutathione Reductase at 2 Angstroms Resolution Authors: Thieme, R. / Pai, E.F. / Schirmer, R.H. / Schulz, G.E. #9: ![]() Title: Gene Duplication in Glutathione Reductase Authors: Schulz, G.E. #10: ![]() Title: The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine Authors: Untucht-Grau, R. / Schulz, G.E. / Schirmer, R.H. #11: ![]() Title: The Structure of the Flavoenzyme Glutathione Reductase Authors: Schulz, G.E. / Schirmer, R.H. / Sachsenheimer, W. / Pai, E.F. #12: ![]() Title: Low Resolution Structure of Human Erythrocyte Glutathione Reductase Authors: Zappe, H.A. / Krohne-Ehrich, G. / Schulz, G.E. #13: ![]() 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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PDBx/mmCIF format | ![]() | 121.1 KB | Display | ![]() |
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PDB format | ![]() | 91 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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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Atom site foot note | 1: RESIDUES PRO 375 AND PRO 468 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 51636.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||
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#2: Chemical | ChemComp-FAD / | ||
#3: Chemical | ChemComp-NDP / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.51 % |
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Crystal grow | Details: THE ENZYME CRYSTAL WAS SOAKED WITH GSSG AND NADP+, DATA WERE COLLECTED, AND THE STRUCTURE OF THE OXIDIZED ENZYME WITH BOUND GSSG AND NADP+ WAS REFINED. THE STRUCTURE CONTAINS 530 WATER ...Details: THE ENZYME CRYSTAL WAS SOAKED WITH GSSG AND NADP+, DATA WERE COLLECTED, AND THE STRUCTURE OF THE OXIDIZED ENZYME WITH BOUND GSSG AND NADP+ WAS REFINED. THE STRUCTURE CONTAINS 530 WATER MOLECULES, 38 DELETED IN RELATION TO FILE 3GRS, 45 ADDED IN RELATION TO FILE 3GRS. |
Crystal grow | *PLUS Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Common name: ammonium sulfate |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||
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Refinement | Resolution: 2→10 Å / σ(F): 0 / Details: THE CRYSTAL STRUCTURE NAME IS E0:GSSG:NADP+. /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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