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基本情報
登録情報 | データベース: PDB / ID: 1gra | |||||||||
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タイトル | SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | |||||||||
![]() | GLUTATHIONE REDUCTASE | |||||||||
![]() | OXIDOREDUCTASE / OXIDOREDUCTASE(FLAVOENZYME) | |||||||||
機能・相同性 | ![]() 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 類似検索 - 分子機能 | |||||||||
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![]() | Karplus, P.A. / Schulz, G.E. | |||||||||
![]() | ![]() タイトル: Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. 著者: Karplus, P.A. / Schulz, G.E. #1: ![]() タイトル: 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 著者: Karplus, P.A. / Krauth-Siegel, R.L. / Schirmer, R.H. / Schulz, G.E. #2: ![]() タイトル: Refined Structure of Glutathione Reductase at 1.54 Angstroms Resolution 著者: Karplus, P.A. / Schulz, G.E. #3: ![]() タイトル: Interaction of a Glutathione S-Conjugate with Glutathione Reductase. Kinetic and X-Ray Crystallographic Studies 著者: Bilzer, M. / Krauth-Siegel, R.L. / Schirmer, R.H. / Akerboom, T.P.M. / Sies, H. / Schulz, G.E. #4: ![]() タイトル: 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 著者: Wierenga, R.K. / Drenth, J. / Schulz, G.E. #5: ![]() タイトル: The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates 著者: Pai, E.F. / Schulz, G.E. #6: ![]() タイトル: Fad-Binding Site of Glutathione Reductase 著者: Schulz, G.E. / Schirmer, R.H. / Pai, E.F. #7: ![]() タイトル: Glutathione Reductase from Human Erythrocytes. The Sequences of the Nadph Domain and of the Interface Domain 著者: Krauth-Siegel, R.L. / Blatterspiel, R. / Saleh, M. / Schiltz, E. / Schirmer, R.H. / Untucht-Grau, R. #8: ![]() タイトル: Three-Dimensional Structure of Glutathione Reductase at 2 Angstroms Resolution 著者: Thieme, R. / Pai, E.F. / Schirmer, R.H. / Schulz, G.E. #10: ![]() タイトル: The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine 著者: Untucht-Grau, R. / Schulz, G.E. / Schirmer, R.H. #11: ![]() タイトル: The Structure of the Flavoenzyme Glutathione Reductase 著者: Schulz, G.E. / Schirmer, R.H. / Sachsenheimer, W. / Pai, E.F. #12: ![]() タイトル: Low Resolution Structure of Human Erythrocyte Glutathione Reductase 著者: Zappe, H.A. / Krohne-Ehrich, G. / Schulz, G.E. #13: ![]() タイトル: Crystals of Human Erythrocyte Glutathione Reductase 著者: Schulz, G.E. / Zappe, H. / Worthington, D.J. / Rosemeyer, M.A. | |||||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDB形式 | ![]() | 91 KB | 表示 | ![]() |
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その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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1 | ![]()
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単位格子 |
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Atom site foot note | 1: RESIDUES PRO 375 AND PRO 468 ARE CIS PROLINES. |
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要素
#1: タンパク質 | 分子量: 51636.242 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() | ||
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#2: 化合物 | ChemComp-FAD / | ||
#3: 化合物 | ChemComp-NDP / | ||
#4: 化合物 | #5: 水 | ChemComp-HOH / | |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.65 Å3/Da / 溶媒含有率: 53.51 % |
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結晶化 | 詳細: 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 ...詳細: 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. |
結晶化 | *PLUS 手法: 蒸気拡散法, ハンギングドロップ法 |
溶液の組成 | *PLUS 一般名: ammonium sulfate |
-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
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解析
ソフトウェア | 名称: TNT / 分類: 精密化 | ||||||||||||
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精密化 | 解像度: 2→10 Å / σ(F): 0 / 詳細: THE CRYSTAL STRUCTURE NAME IS E0:GSSG:NADP+. /
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精密化ステップ | サイクル: LAST / 解像度: 2→10 Å
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