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- PDB-2vm1: Crystal structure of barley thioredoxin h isoform 1 crystallized ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vm1 | ||||||
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Title | Crystal structure of barley thioredoxin h isoform 1 crystallized using ammonium sulfate as precipitant | ||||||
![]() | THIOREDOXIN H ISOFORM 1. | ||||||
![]() | OXIDOREDUCTASE / PROTEIN DISULFIDE REDUCTASE / THIOREDOXIN-FOLD | ||||||
Function / homology | ![]() plasmodesmata-mediated intercellular transport / oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor / enzyme inhibitor activity / protein-disulfide reductase activity / response to cold / response to oxidative stress / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Maeda, K. / Hagglund, P. / Finnie, C. / Svensson, B. / Henriksen, A. | ||||||
![]() | ![]() Title: Crystal Structures of Barley Thioredoxin H Isoforms Hvtrxh1 and Hvtrxh2 Reveal Features Involved in Protein Recognition and Possibly in Discriminating the Isoform Specificity. Authors: Maeda, K. / Hagglund, P. / Finnie, C. / Svensson, B. / Henriksen, 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 | ![]() | 103.2 KB | Display | ![]() |
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PDB format | ![]() | 85.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.7 KB | Display | ![]() |
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Full document | ![]() | 442.8 KB | Display | |
Data in XML | ![]() | 22.8 KB | Display | |
Data in CIF | ![]() | 33.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 12769.681 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Variant: BARKE / Plasmid: PET11A / Production host: ![]() ![]() References: UniProt: Q7XZK3, thioredoxin-disulfide reductase #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.61 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20.5 Å / Num. obs: 53797 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 9 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 1.6 / % possible all: 96 |
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Processing
Software | Name: REFMAC / Version: 5.2.0005 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]()
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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: 17.46 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→121.27 Å
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Refine LS restraints |
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