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Open data
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Basic information
Entry | Database: PDB / ID: 1xwc | ||||||
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Title | Drosophila thioredoxin, reduced, P6522 | ||||||
![]() | thioredoxin | ||||||
![]() | ELECTRON TRANSPORT / Dimerization / Drosophila melanogaster / redox regulation / thioredoxin / x-ray crystal structure | ||||||
Function / homology | ![]() The NLRP3 inflammasome / TP53 Regulates Metabolic Genes / Protein repair / Detoxification of Reactive Oxygen Species / Interconversion of nucleotide di- and triphosphates / Oxidative Stress Induced Senescence / glutathione disulfide oxidoreductase activity / disulfide oxidoreductase activity / protein-disulfide reductase activity / defense response to fungus ...The NLRP3 inflammasome / TP53 Regulates Metabolic Genes / Protein repair / Detoxification of Reactive Oxygen Species / Interconversion of nucleotide di- and triphosphates / Oxidative Stress Induced Senescence / glutathione disulfide oxidoreductase activity / disulfide oxidoreductase activity / protein-disulfide reductase activity / defense response to fungus / cell redox homeostasis / determination of adult lifespan / response to oxidative stress / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wahl, M.C. / Irmler, A. / Hecker, B. / Schirmer, R.H. / Becker, K. | ||||||
![]() | ![]() Title: Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster Authors: Wahl, M.C. / Irmler, A. / Hecker, B. / Schirmer, R.H. / Becker, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 32.3 KB | Display | ![]() |
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PDB format | ![]() | 21.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.4 KB | Display | ![]() |
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Full document | ![]() | 420.3 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 8.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1xw9C ![]() 1xwaC ![]() 1xwbC ![]() 1aucS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 11748.636 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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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 51.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 8.5 Details: ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 5951 / % possible obs: 95.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 47.1 Å2 / Rsym value: 0.07 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 2.3→2.4 Å / % possible all: 95.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB Entry 1AUC Resolution: 2.3→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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