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Yorodumi- PDB-3trx: HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINAN... -
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-Basic information
Entry | Database: PDB / ID: 3trx | ||||||
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Title | HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINANT HUMAN THIOREDOXIN IN SOLUTION | ||||||
Components | THIOREDOXIN | ||||||
Keywords | ELECTRON TRANSPORT | ||||||
Function / homology | Function and homology information Protein repair / cellular detoxification of hydrogen peroxide / protein-disulfide reductase (NAD(P)H) activity / positive regulation of peptidyl-cysteine S-nitrosylation / Interconversion of nucleotide di- and triphosphates / thioredoxin-disulfide reductase (NADPH) activity / 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 / protein-disulfide reductase (NAD(P)H) activity / positive regulation of peptidyl-cysteine S-nitrosylation / Interconversion of nucleotide di- and triphosphates / thioredoxin-disulfide reductase (NADPH) activity / negative regulation of protein export from nucleus / Regulation of FOXO transcriptional activity by acetylation / NFE2L2 regulating anti-oxidant/detoxification enzymes / response to nitric oxide / positive regulation of DNA binding / Detoxification of Reactive Oxygen Species / The NLRP3 inflammasome / protein-disulfide reductase activity / Purinergic signaling in leishmaniasis infection / activation of protein kinase B activity / cell redox homeostasis / TP53 Regulates Metabolic Genes / response to radiation / positive regulation of peptidyl-serine phosphorylation / 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 Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Forman-Kay, J.D. / Clore, G.M. / Gronenborn, A.M. | ||||||
Citation | Journal: Biochemistry / Year: 1991 Title: High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Authors: Forman-Kay, J.D. / Clore, G.M. / Wingfield, P.T. / Gronenborn, A.M. #1: Journal: Biochemistry / Year: 1990 Title: Studies on the Solution Conformation of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy Authors: Forman-Kay, J.D. / Gronenborn, A.M. / Kay, L.E. / Wingfield, P.T. / Clore, G.M. #2: Journal: Biochemistry / Year: 1989 Title: A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin Authors: Forman-Kay, J.D. / Clore, G.M. / Driscoll, P.C. / Wingfield, P. / Richards, F.M. / Gronenborn, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3trx.cif.gz | 45.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3trx.ent.gz | 33.3 KB | Display | PDB format |
PDBx/mmJSON format | 3trx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3trx_validation.pdf.gz | 241.9 KB | Display | wwPDB validaton report |
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Full document | 3trx_full_validation.pdf.gz | 241.7 KB | Display | |
Data in XML | 3trx_validation.xml.gz | 3.8 KB | Display | |
Data in CIF | 3trx_validation.cif.gz | 4.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tr/3trx ftp://data.pdbj.org/pub/pdb/validation_reports/tr/3trx | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: RESIDUE PRO 75 IS A CIS PROLINE. | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 11720.387 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P10599 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Processing
Refinement | Software ordinal: 1 Details: 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 ...Details: 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. |
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NMR ensemble | Conformers submitted total number: 1 |