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- PDB-1trs: THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE ... -
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Basic information
Entry | Database: PDB / ID: 1trs | ||||||
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Title | THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN | ||||||
![]() | THIOREDOXIN![]() | ||||||
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Function / homology | ![]() Protein repair / cellular detoxification of hydrogen peroxide / positive regulation of peptidyl-cysteine S-nitrosylation / 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 / NFE2L2 regulating anti-oxidant/detoxification enzymes / response to nitric oxide ...Protein repair / cellular detoxification of hydrogen peroxide / positive regulation of peptidyl-cysteine S-nitrosylation / 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 / NFE2L2 regulating anti-oxidant/detoxification enzymes / response to nitric oxide / Detoxification of Reactive Oxygen Species / The NLRP3 inflammasome / ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Clore, G.M. / Qin, J. / Gronenborn, A.M. | ||||||
![]() | ![]() Title: The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Authors: Qin, J. / Clore, G.M. / Gronenborn, A.M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 42.4 KB | Display | ![]() |
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PDB format | ![]() | 33.7 KB | Display | ![]() |
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-Validation report
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-Related structure data
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Assembly
Deposited unit | ![]()
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Atom site foot note | 1: CIS PROLINE - PRO 75 | |||||||||
NMR ensembles |
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Components
#1: Protein | ![]() Mass: 11624.190 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Processing
Refinement | Software ordinal: 1 Details: THE 3D STRUCTURE OF OXIDIZED HUMAN THIOREDOXIN IN SOLUTION BY NMR IS BASED ON 3018 EXPERIMENTAL RESTRAINTS COMPRISING: 2649 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS; 34 RESTRAINTS ...Details: THE 3D STRUCTURE OF OXIDIZED HUMAN THIOREDOXIN IN SOLUTION BY NMR IS BASED ON 3018 EXPERIMENTAL RESTRAINTS COMPRISING: 2649 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS; 34 RESTRAINTS FOR 17 H-BONDS INVOLVING 7 TIGHTLY BOUND WATER MOLECULES; 42 RESTRAINTS FOR 21 BACKBONE HYDROGEN BONDS INVOLVING SLOWLY EXCHANGING AMIDE PROTONS; 278 TORSION ANGLE RESTRAINTS (104 PHI, 76 PSI, 78 CHI1 AND 20 CHI2); AND 91 HN-HALPHA THREE-BOND COUPLING CONSTANTS. A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS AND 1H, 13C AND 15N ASSIGNMENTS HAVE BEEN DEPOSITED WITH THE PROTEIN DATA BANK. THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. & GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324. ALL STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE. THIS ENTRY CONTAINS THE RESTRAINED MINIMIZED AVERAGE STRUCTURE (SA)R. THIS IS OBTAINED BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 40 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES 1 - 105 AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE 40 INDIVIDUAL STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1TRU. COLUMNS 61 - 65 OF THE COORDINATE RECORDS (THE B VALUE FIELD IN X-RAY STRUCTURES) IN THE MINIMIZED STRUCTURE (ENTRY 1TRS) GIVE THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE NUMBERS IN THIS FIELD OF THE INDIVIDUAL STRUCTURES (ENTRY 1TRU) HAVE NO MEANING. |
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NMR ensemble | Conformers submitted total number: 1 |