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- PDB-7bvv: Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7bvv | ||||||
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Title | Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 | ||||||
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![]() | OXIDOREDUCTASE / peroxiredoxin / thioredoxin / alkyl hydroperoxide reductase / complex | ||||||
Function / homology | ![]() membrane fusion priming complex / protein deglutathionylation / TP53 Regulates Metabolic Genes / Interconversion of nucleotide di- and triphosphates / vacuole inheritance / The NLRP3 inflammasome / vacuole fusion, non-autophagic / sulfate assimilation / disulfide oxidoreductase activity / Detoxification of Reactive Oxygen Species ...membrane fusion priming complex / protein deglutathionylation / TP53 Regulates Metabolic Genes / Interconversion of nucleotide di- and triphosphates / vacuole inheritance / The NLRP3 inflammasome / vacuole fusion, non-autophagic / sulfate assimilation / disulfide oxidoreductase activity / Detoxification of Reactive Oxygen Species / thioredoxin-dependent peroxiredoxin / thioredoxin peroxidase activity / fungal-type vacuole / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / deoxyribonucleotide biosynthetic process / Oxidative Stress Induced Senescence / response to metal ion / protein-disulfide reductase activity / endoplasmic reticulum to Golgi vesicle-mediated transport / glutathione metabolic process / cell redox homeostasis / hydrogen peroxide catabolic process / peroxisome / protein transport / cellular response to oxidative stress / Golgi membrane / mitochondrion / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lian, F.M. / Jiang, Y.L. / Yang, W. / Yang, X. | ||||||
![]() | ![]() Title: Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 mimics a conformational intermediate during the catalytic cycle. Authors: Lian, F.M. / Jiang, Y.L. / Yang, W. / Yang, X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 71 KB | Display | ![]() |
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PDB format | ![]() | 50.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.7 KB | Display | ![]() |
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Full document | ![]() | 433.8 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 17.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4dssS 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 19180.598 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: AHP1, YLR109W, L2916, L9354.5 / Production host: ![]() ![]() |
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#2: Protein | Mass: 12214.898 Da / Num. of mol.: 1 / Mutation: C34S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: TRX2, TRX1, YGR209C, G7746 / Production host: ![]() ![]() |
#3: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.72 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 25% polyethylene glycol 3,350, 0.2 M lithium sulfate, 0.1 M HEPES-NaOH, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 13, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.12→50 Å / Num. obs: 16850 / % possible obs: 100 % / Redundancy: 7.1 % / Biso Wilson estimate: 30.1 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.087 / Rpim(I) all: 0.035 / Rrim(I) all: 0.094 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 2.12→2.23 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.493 / Mean I/σ(I) obs: 4.2 / Num. unique obs: 2424 / CC1/2: 0.904 / Rpim(I) all: 0.195 / Rrim(I) all: 0.53 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4DSS Resolution: 2.12→38.525 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.921 / Cross valid method: THROUGHOUT / ESU R: 0.252 / ESU R Free: 0.195 Details: Hydrogens have been added in their 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.033 Å2
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Refinement step | Cycle: LAST / Resolution: 2.12→38.525 Å
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Refine LS restraints |
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LS refinement shell |
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