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Open data
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Basic information
Entry | Database: PDB / ID: 1w89 | ||||||
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Title | Structure of the reduced form of human thioredoxin 2 | ||||||
![]() | THIOREDOXIN | ||||||
![]() | ELECTRON TRANSPORT / ANTIOXIDANT ENZYME / 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 | ![]() | 145.3 KB | Display | ![]() |
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PDB format | ![]() | 116.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 479.1 KB | Display | ![]() |
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Full document | ![]() | 484.7 KB | Display | |
Data in XML | ![]() | 29.8 KB | Display | |
Data in CIF | ![]() | 44 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uvzSC ![]() 1w4vC S: Starting model for refinement C: citing same article ( |
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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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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 13288.154 Da / Num. of mol.: 6 / Fragment: ACTIVE SITE, RESIDUES 60-166 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | THR1 CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.6 % |
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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. SOACKING IN A TRISHYDROXIMETHYLPHOSPHINE SOLUTION 10MM |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 1, 2004 / Details: BENT MIRROR |
Radiation | Monochromator: DOUBLE CRYSTAL FOCUSSING MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 2→19.4 Å / Num. obs: 50114 / % possible obs: 97.1 % / Observed criterion σ(I): 0 / Redundancy: 2.68 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.42 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 2.53 % / Rmerge(I) obs: 0.24 / Mean I/σ(I) obs: 4.29 / % possible all: 97.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1UVZ Resolution: 2→19.23 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.88 / SU B: 11.824 / SU ML: 0.171 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.215 / ESU R Free: 0.203 / 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: 15.23 Å2
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Refinement step | Cycle: LAST / Resolution: 2→19.23 Å
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Refine LS restraints |
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