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Open data
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Basic information
Entry | Database: PDB / ID: 1uvz | ||||||
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Title | structure of human thioredoxin 2 | ||||||
![]() | THIOREDOXIN | ||||||
![]() | OXIDOREDUCTASE / THIOREDOXIN / MITOCHONDRION | ||||||
Function / homology | ![]() peptide-methionine (R)-S-oxide reductase activity / Degradation of cysteine and homocysteine / peptide-methionine (S)-S-oxide reductase activity / Detoxification of Reactive Oxygen Species / cellular response to nutrient levels / protein-disulfide reductase activity / response to axon injury / response to glucose / cell redox homeostasis / response to hormone ...peptide-methionine (R)-S-oxide reductase activity / Degradation of cysteine and homocysteine / peptide-methionine (S)-S-oxide reductase activity / Detoxification of Reactive Oxygen Species / cellular response to nutrient levels / protein-disulfide reductase activity / response to axon injury / response to glucose / cell redox homeostasis / response to hormone / response to organic cyclic compound / response to oxidative stress / response to hypoxia / mitochondrial matrix / response to xenobiotic stimulus / neuronal cell body / dendrite / protein-containing complex binding / nucleolus / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Smeets, A. / Evrard, C. / Declercq, J.P. | ||||||
![]() | ![]() Title: Crystal Structures of Oxidized and Reduced Forms of Human Mitochondrial Thioredoxin 2. Authors: Smeets, A. / Evrard, C. / Landtmeters, M. / Marchand, C. / Knoops, B. / Declercq, J.P. #1: Journal: J.Biol.Chem. / Year: 2002 Title: Human Mitochondrial Thioredoxin Authors: Damdimopoulos, A.E. / Miranda-Vizuete, A. / Pelto-Huikkos, M. / Gustafsson, J.A. / Spyrou, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.2 KB | Display | ![]() |
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PDB format | ![]() | 116.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 468 KB | Display | ![]() |
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Full document | ![]() | 477.8 KB | Display | |
Data in XML | ![]() | 31.1 KB | Display | |
Data in CIF | ![]() | 45.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w4vC ![]() 1w89C ![]() 1ertS 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 13288.154 Da / Num. of mol.: 6 / Fragment: RESIDUES 60-166 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | AMINO ACID NUMBERING STARTS AT THR1 WHICH IS THE FIRST AMINO ACID OF THE PROCESSED PROTEIN WITHOUT ...AMINO ACID NUMBERING STARTS AT THR1 WHICH IS THE FIRST AMINO ACID OF THE PROCESSED PROTEIN WITHOUT ITS MITOCHONDR | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 45.8 % |
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Crystal grow | pH: 4.6 Details: PEG 3350 22% (W/V), NA ACETATE 0.1M (PH: 4.6), AMMONIUM SULFATE 0.2M, DTT 1MM, pH 4.60 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 2, 2002 / Details: BENT MIRROR |
Radiation | Monochromator: TRIANGULAR MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8441 Å / Relative weight: 1 |
Reflection | Resolution: 2→23.5 Å / Num. obs: 47020 / % possible obs: 96.9 % / Redundancy: 2.11 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 9.72 |
Reflection shell | Resolution: 2→2.2 Å / Redundancy: 2 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 4.22 / % possible all: 90.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ERT Resolution: 2.01→23.25 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.9 / SU B: 5.578 / SU ML: 0.153 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.206 / ESU R Free: 0.193 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE DISTANCES OBSERVED IN THE 3 MOLECULES BETWEEN THE CYSTEINYL SULFUR ATOMS (CYS 31 AND CYS 34) IS HALFWAY BETWEEN THE VALUE REQUIRED FOR ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE DISTANCES OBSERVED IN THE 3 MOLECULES BETWEEN THE CYSTEINYL SULFUR ATOMS (CYS 31 AND CYS 34) IS HALFWAY BETWEEN THE VALUE REQUIRED FOR THE FORMATION OF A DISULFIDE BOND (OXIDIZED FORM) AND THE VALUE REQUIRED IN THE ABSENCE OF SUCH A BOND (SUM OF VDW RADII IN THE REDUCED FORM). AN HYPOTHESIS COULD BE THAT ALTERNATE CONFORMATIONS (OXIDIZED AND REDUCED) COEXIST, BUT THE RESOLUTION ACHIEVED IS NOT HIGH ENOUGH TO OBSERVE ALTERNATE CONFORMATIONS. THE ELECTRON DENSITY IS THUS AN AVERAGE DENSITY BETWEEN BOTH CONFORMATIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 12.82 Å2
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Refinement step | Cycle: LAST / Resolution: 2.01→23.25 Å
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Refine LS restraints |
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