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Open data
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Basic information
Entry | Database: PDB / ID: 1h6v | ||||||
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Title | Mammalian thioredoxin reductase | ||||||
![]() | THIOREDOXIN REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE / FLAVOPROTEIN | ||||||
Function / homology | ![]() selenate reductase activity / halogen metabolic process / Metabolism of ingested MeSeO2H into MeSeH / benzene-containing compound metabolic process / Interconversion of nucleotide di- and triphosphates / Detoxification of Reactive Oxygen Species / NADPH peroxidase / NADPH peroxidase activity / cellular response to hyperoxia / TP53 Regulates Metabolic Genes ...selenate reductase activity / halogen metabolic process / Metabolism of ingested MeSeO2H into MeSeH / benzene-containing compound metabolic process / Interconversion of nucleotide di- and triphosphates / Detoxification of Reactive Oxygen Species / NADPH peroxidase / NADPH peroxidase activity / cellular response to hyperoxia / TP53 Regulates Metabolic Genes / NADPH oxidation / mercury ion binding / NAD(P)H oxidase H2O2-forming activity / selenocysteine metabolic process / thioredoxin-disulfide reductase / response to selenium ion / glutathione-disulfide reductase (NADPH) activity / thioredoxin-disulfide reductase (NADPH) activity / mesoderm formation / response to axon injury / response to hyperoxia / gastrulation / cellular response to copper ion / FAD binding / glutathione metabolic process / cell redox homeostasis / hydrogen peroxide catabolic process / cellular response to oxidative stress / response to oxidative stress / cell population proliferation / response to xenobiotic stimulus / positive regulation of apoptotic process / neuronal cell body / mitochondrion / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sandalova, T. / Zhong, L. / Lindqvist, Y. / Holmgren, A. / Schneider, G. | ||||||
![]() | ![]() Title: Three-Dimensional Structure of a Mammalian Thioredoxin Reductase: Implication for Mechanism and Evolution of a Selenocysteine Dependent Enzyme Authors: Sandalova, T. / Zhong, L. / Lindqvist, Y. / Holmgren, A. / Schneider, G. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: Purification, Crystallization and Preliminarycrystallographic Data for Rat Cytosolic Selenocysteine 498 - Cysteine Mutant Thioredoxin Reductase Authors: Zhong, L. / Persson, K. / Sandalova, T. / Schneider, G. / Holmgren, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 556.6 KB | Display | ![]() |
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PDB format | ![]() | 457.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.7 MB | Display | ![]() |
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Full document | ![]() | 3.1 MB | Display | |
Data in XML | ![]() | 128.8 KB | Display | |
Data in CIF | ![]() | 167.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1graS 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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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 54646.305 Da / Num. of mol.: 6 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-FAD / #3: Chemical | ChemComp-NDP / #4: Water | ChemComp-HOH / | Compound details | CHAIN A, B, C, D, E, F ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 56.65 % |
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Crystal grow | pH: 7.5 Details: 20% PEG 8000 IN 50MM POTASSIUM PHOSPHATE, PH 5.0 AND 2MM OF NADP+ |
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Zhong, L., (2000) Acta Crystallogr.,Sect.D, 56, 1191. |
Components of the solutions | *PLUS Conc.: 60 mg/ml / Common name: enzyme |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.104 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. obs: 69351 / % possible obs: 92.7 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.095 / Net I/σ(I): 11 |
Reflection shell | Resolution: 3→3.05 Å / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 7 / % possible all: 77.6 |
Reflection | *PLUS Num. measured all: 212337 |
Reflection shell | *PLUS % possible obs: 77.6 % / Mean I/σ(I) obs: 2.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GRA Resolution: 3→30 Å / SU B: 20.412 / SU ML: 0.385 / Cross valid method: THROUGHOUT / ESU R Free: 0.486 / Details: CHAINS A, B, E, AND F ARE BETTER
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Refinement step | Cycle: LAST / Resolution: 3→30 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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