+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 3trx | ||||||
---|---|---|---|---|---|---|---|
タイトル | HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINANT HUMAN THIOREDOXIN IN SOLUTION | ||||||
![]() | THIOREDOXIN | ||||||
![]() | ELECTRON TRANSPORT | ||||||
機能・相同性 | ![]() positive regulation of peptidyl-cysteine S-nitrosylation / Protein repair / cellular detoxification of hydrogen peroxide / protein-disulfide reductase [NAD(P)H] activity / thioredoxin-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / negative regulation of protein export from nucleus / Regulation of FOXO transcriptional activity by acetylation / positive regulation of DNA binding / NFE2L2 regulating anti-oxidant/detoxification enzymes ...positive regulation of peptidyl-cysteine S-nitrosylation / Protein repair / cellular detoxification of hydrogen peroxide / protein-disulfide reductase [NAD(P)H] activity / thioredoxin-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / negative regulation of protein export from nucleus / Regulation of FOXO transcriptional activity by acetylation / positive regulation of DNA binding / NFE2L2 regulating anti-oxidant/detoxification enzymes / response to nitric oxide / Detoxification of Reactive Oxygen Species / The NLRP3 inflammasome / protein-disulfide reductase activity / Purinergic signaling in leishmaniasis infection / cell redox homeostasis / TP53 Regulates Metabolic Genes / response to radiation / Oxidative Stress Induced Senescence / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR | ||||||
![]() | Forman-Kay, J.D. / Clore, G.M. / Gronenborn, A.M. | ||||||
![]() | ![]() タイトル: High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. 著者: Forman-Kay, J.D. / Clore, G.M. / Wingfield, P.T. / Gronenborn, A.M. #1: ![]() タイトル: Studies on the Solution Conformation of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy 著者: Forman-Kay, J.D. / Gronenborn, A.M. / Kay, L.E. / Wingfield, P.T. / Clore, G.M. #2: ![]() タイトル: A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin 著者: Forman-Kay, J.D. / Clore, G.M. / Driscoll, P.C. / Wingfield, P. / Richards, F.M. / Gronenborn, A.M. | ||||||
履歴 |
|
-
構造の表示
構造ビューア | 分子: ![]() ![]() |
---|
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 45.9 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 33.3 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 241.9 KB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 241.7 KB | 表示 | |
XML形式データ | ![]() | 3.8 KB | 表示 | |
CIF形式データ | ![]() | 4.8 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
-
リンク
-
集合体
登録構造単位 | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
Atom site foot note | 1: RESIDUE PRO 75 IS A CIS PROLINE. | |||||||||
NMR アンサンブル |
|
-
要素
#1: タンパク質 | 分子量: 11720.387 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() |
---|
-実験情報
-実験
実験 | 手法: 溶液NMR |
---|
-
解析
精密化 | ソフトェア番号: 1 詳細: STRUCTURES DETERMINED BY THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD OF M. NILGES, G. M. CLORE, AND A. M. GRONENBORN (FEBS LETT. 229, 317 (1988)). THE ...詳細: STRUCTURES DETERMINED BY THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD OF M. NILGES, G. M. CLORE, AND A. M. GRONENBORN (FEBS LETT. 229, 317 (1988)). THE STRUCTURES ARE BASED ON 1983 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 52 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 26 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE CALCULATIONS; AND 98 PHI AND 71 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 72 CHI1 SIDE-CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE DATA. A TOTAL OF 33 STRUCTURES WERE CALCULATED. THIS STRUCTURE REPRESENTS THE MINIMIZED AVERAGE STRUCTURE. THIS IS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE ENTIRE SET OF 33 STRUCTURES CAN BE FOUND IN PDB ENTRY 4TRX. THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS. |
---|---|
NMRアンサンブル | 登録したコンフォーマーの数: 1 |