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- PDB-2hsy: Solution structure of Thioredoxin 2 from Saccharomyces cerevisiae -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hsy | ||||||
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Title | Solution structure of Thioredoxin 2 from Saccharomyces cerevisiae | ||||||
![]() | Thioredoxin II | ||||||
![]() | OXIDOREDUCTASE / thioredoxin | ||||||
Function / homology | ![]() membrane fusion priming complex / protein deglutathionylation / TP53 Regulates Metabolic Genes / Interconversion of nucleotide di- and triphosphates / vacuole inheritance / The NLRP3 inflammasome / vacuole fusion, non-autophagic / sulfate assimilation / disulfide oxidoreductase activity / Detoxification of Reactive Oxygen Species ...membrane fusion priming complex / protein deglutathionylation / TP53 Regulates Metabolic Genes / Interconversion of nucleotide di- and triphosphates / vacuole inheritance / The NLRP3 inflammasome / vacuole fusion, non-autophagic / sulfate assimilation / disulfide oxidoreductase activity / Detoxification of Reactive Oxygen Species / fungal-type vacuole / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / deoxyribonucleotide biosynthetic process / Oxidative Stress Induced Senescence / protein-disulfide reductase activity / endoplasmic reticulum to Golgi vesicle-mediated transport / glutathione metabolic process / cell redox homeostasis / protein transport / Golgi membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
![]() | Amorim, G.C. / Valente, A.P. / Almeida, F.C.L. | ||||||
![]() | ![]() Title: NMR solution structure of the reduced form of thioredoxin 2 from Saccharomyces cerevisiae Authors: Amorim, G.C. / Pinheiro, A.S. / Netto, L.E.S. / Valente, A.P. / Almeida, F.C.L. #1: Journal: J.Biomol.Nmr / Year: 2006 Title: (1)H, (13)C and (15)N Resonance Assignments for the Reduced Forms of Thioredoxin 1 and 2 from S. cerevisiae Authors: Pinheiro, A.S. / Amorim, G.C. / Netto, L.E.S. / Valente, A.P. / Almeida, F.C.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 609.2 KB | Display | ![]() |
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PDB format | ![]() | 508.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 342.3 KB | Display | ![]() |
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Full document | ![]() | 489.1 KB | Display | |
Data in XML | ![]() | 43 KB | Display | |
Data in CIF | ![]() | 66.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 11213.836 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pET17b / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 20mM phosphate buffer Na; 10mM DTT; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0 / pH: 7.0 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software | Name: CNS / Version: 1.1 / Classification: refinement |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 / Details: cartesian simulated annealing |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |