+Open data
-Basic information
Entry | Database: PDB / ID: 1xwc | ||||||
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Title | Drosophila thioredoxin, reduced, P6522 | ||||||
Components | thioredoxin | ||||||
Keywords | ELECTRON TRANSPORT / Dimerization / Drosophila melanogaster / redox regulation / thioredoxin / x-ray crystal structure | ||||||
Function / homology | Function and homology information 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 Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Wahl, M.C. / Irmler, A. / Hecker, B. / Schirmer, R.H. / Becker, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xwc.cif.gz | 32.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xwc.ent.gz | 21.9 KB | Display | PDB format |
PDBx/mmJSON format | 1xwc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xwc_validation.pdf.gz | 417.4 KB | Display | wwPDB validaton report |
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Full document | 1xwc_full_validation.pdf.gz | 420.3 KB | Display | |
Data in XML | 1xwc_validation.xml.gz | 7 KB | Display | |
Data in CIF | 1xwc_validation.cif.gz | 8.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xw/1xwc ftp://data.pdbj.org/pub/pdb/validation_reports/xw/1xwc | HTTPS FTP |
-Related structure data
Related structure data | 1xw9C 1xwaC 1xwbC 1aucS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-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.) Drosophila melanogaster (fruit fly) / Gene: TRX-2 / Plasmid: pQE-30 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9V429 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
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 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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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