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Open data
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Basic information
Entry | Database: PDB / ID: 1aog | ||||||
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Title | TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE (OXIDIZED FORM) | ||||||
![]() | TRYPANOTHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / TRYPANOTHIONE REDUCTASE / FAD DEPENDENT DISULPHIDE OXIDOREDUCTASE | ||||||
Function / homology | ![]() trypanothione-disulfide reductase / trypanothione-disulfide reductase (NADPH) activity / glutathione-disulfide reductase (NADPH) activity / glutathione metabolic process / cell redox homeostasis / flavin adenine dinucleotide binding / cellular response to oxidative stress / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bond, C.S. / Zhang, Y. / Hunter, W.N. | ||||||
![]() | ![]() Title: The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Authors: Zhang, Y. / Bond, C.S. / Bailey, S. / Cunningham, M.L. / Fairlamb, A.H. / Hunter, W.N. #1: ![]() Title: Site-Directed Mutagenesis of the Redox-Active Cysteines of Trypanosoma Cruzi Trypanothione Reductase Authors: Borges, A. / Cunningham, M.L. / Tovar, J. / Fairlamb, A.H. #2: ![]() Title: Trypanosoma Cruzi Trypanothione Reductase Crystallisation, Unit Cell Dimensions and Structure Solution Authors: Zhang, Y. / Bailey, S. / Naismith, J.H. / Bond, C.S. / Habash, J. / Mclaughlin, P. / Papiz, M.Z. / Borges, A. / Cunningham, M.L. / Fairlamb, A.H. / Hunter, W.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 209.9 KB | Display | ![]() |
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PDB format | ![]() | 165.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1tytS 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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Unit cell |
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Components
#1: Protein | Mass: 53175.773 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.17 Å3/Da / Density % sol: 61.21 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 6-8 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Mar 1, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. obs: 55392 / % possible obs: 94.1 % / Observed criterion σ(I): 1 / Redundancy: 3.1 % / Rmerge(I) obs: 0.109 |
Reflection | *PLUS Num. measured all: 170106 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.4 Å / % possible obs: 80 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1TYT Resolution: 2.3→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 32.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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