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Open data
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Basic information
Entry | Database: PDB / ID: 2jk6 | ||||||
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Title | Structure of Trypanothione Reductase from Leishmania infantum | ||||||
![]() | TRYPANOTHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / OXIDANT DETOXIFICATION / TRYPANOTHIONE METABOLISM / FAD / LEISHMANIA / TRYPANOSOMA / ANTIMONIALS / FLAVOPROTEIN / REDOX-ACTIVE CENTER | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Baiocco, P. / Colotti, G. / Franceschini, S. / Ilari, A. | ||||||
![]() | ![]() Title: Molecular Basis of Antimony Treatment in Leishmaniasis. Authors: Baiocco, P. / Colotti, G. / Franceschini, S. / Ilari, A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 196.3 KB | Display | ![]() |
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PDB format | ![]() | 154.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 987.2 KB | Display | ![]() |
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Full document | ![]() | 997 KB | Display | |
Data in XML | ![]() | 34.9 KB | Display | |
Data in CIF | ![]() | 47.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2w0hC ![]() 1feaS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Refine code: 2
NCS ensembles :
NCS oper: (Code: given Matrix: (0.00044, -1, -0.00029), Vector: |
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Components
#1: Protein | Mass: 55257.547 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: A4HSF7, trypanothione-disulfide reductase #2: Chemical | #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | Sequence details | IN THE STRUCTURE THE FIRST 20 AMINOACID ARE MISSING | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.67 Å3/Da / Density % sol: 74 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 2.2 M AMMONIUM SULPHATE, 0.1 M TRIS PH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 2, 2008 |
Radiation | Monochromator: KMC-2 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 2.95→103 Å / Num. obs: 41850 / % possible obs: 99 % / Observed criterion σ(I): 2 / Redundancy: 4.8 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 23 |
Reflection shell | Resolution: 2.95→3 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 3.8 / % possible all: 84 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FEA Resolution: 2.95→103.69 Å / Cor.coef. Fo:Fc: 0.916 / Cor.coef. Fo:Fc free: 0.89 / SU B: 14.313 / SU ML: 0.257 / Cross valid method: THROUGHOUT / ESU R: 0.655 / ESU R Free: 0.352 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.78 Å2
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Refinement step | Cycle: LAST / Resolution: 2.95→103.69 Å
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Refine LS restraints |
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