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Open data
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Basic information
Entry | Database: PDB / ID: 5b8b | ||||||
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Title | Crystal structure of reduced chimeric E.coli AhpC1-186-YFSKHN | ||||||
![]() | Alkyl hydroperoxide reductase subunit C,Peroxiredoxin-2 | ||||||
![]() | OXIDOREDUCTASE / Alkylhydroperoxide reductase / AhpC / Peroxiredoxins / chimeric | ||||||
Function / homology | ![]() response to alkyl hydroperoxide / respiratory burst involved in inflammatory response / alkyl hydroperoxide reductase complex / peptidyl-histidine phosphorylation / hydroperoxide reductase activity / cellular response to sulfate starvation / NADH-dependent peroxiredoxin / NADH-dependent peroxiredoxin activity / leukocyte activation / negative regulation of T cell differentiation ...response to alkyl hydroperoxide / respiratory burst involved in inflammatory response / alkyl hydroperoxide reductase complex / peptidyl-histidine phosphorylation / hydroperoxide reductase activity / cellular response to sulfate starvation / NADH-dependent peroxiredoxin / NADH-dependent peroxiredoxin activity / leukocyte activation / negative regulation of T cell differentiation / siderophore biosynthetic process / oxidoreductase activity, acting on peroxide as acceptor / regulation of hydrogen peroxide metabolic process / thioredoxin-dependent peroxiredoxin / negative regulation of lipopolysaccharide-mediated signaling pathway / thioredoxin peroxidase activity / defense response to tumor cell / response to hydroperoxide / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / Detoxification of Reactive Oxygen Species / T cell homeostasis / antioxidant activity / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of blood coagulation / T cell proliferation / extrinsic apoptotic signaling pathway / removal of superoxide radicals / thymus development / cell redox homeostasis / hydrogen peroxide catabolic process / TP53 Regulates Metabolic Genes / peroxidase activity / cellular response to oxidative stress / regulation of apoptotic process / response to oxidative stress / response to lipopolysaccharide / positive regulation of MAPK cascade / negative regulation of apoptotic process / extracellular exosome / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kamariah, N. / Sek, M.F. / Eisenhaber, B. / Eisenhaber, F. / Gruber, G. | ||||||
![]() | ![]() Title: Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins. Authors: Kamariah, N. / Sek, M.F. / Eisenhaber, B. / Eisenhaber, F. / Gruber, G. #1: ![]() Title: The ups and downs in AhpF: Structure, mechanism and ensemble formation of the Alkylhydroperoxide Reductase subunits AhpC and AhpF from Escherichia coli Authors: Dip, P.V. / Kamariah, N. / Manimekalai, M.S.S. / Nartey, W. / Balakrishna, A.M. / Eisenhaber, F. / Eisenhaber, B. / Gruber, 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 | ![]() | 654.1 KB | Display | ![]() |
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PDB format | ![]() | 553 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 510.8 KB | Display | ![]() |
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Full document | ![]() | 516.7 KB | Display | |
Data in XML | ![]() | 52.2 KB | Display | |
Data in CIF | ![]() | 71 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5b8aC ![]() 1n8jS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 4 / Auth seq-ID: 1 - 160 / Label seq-ID: 1 - 160
NCS oper:
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Components
#1: Protein | Mass: 21452.109 Da / Num. of mol.: 10 / Fragment: UNP RESIDUES 1-186,UNP RESIDUES 193-198 Source method: isolated from a genetically manipulated source Details: The fusion protein of E.coli AhpC (residues 1-186) and human Prx2 (residues 193-198) Source: (gene. exp.) ![]() ![]() ![]() Strain: K12 / Gene: ahpC, b0605, JW0598, PRDX2, NKEFB, TDPX1 / Production host: ![]() ![]() #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: 3.15 Å3/Da / Density % sol: 61 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 1.6 M ammonium sulfate, 100 mM MES pH 6.5, 5% Dioxane |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 16, 2015 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.999999 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. obs: 44808 / % possible obs: 92.9 % / Redundancy: 3.1 % / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 2.9 % / % possible all: 92 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1N8J Resolution: 3.1→50 Å / Cor.coef. Fo:Fc: 0.881 / Cor.coef. Fo:Fc free: 0.847 / SU B: 61.738 / Cross valid method: THROUGHOUT / ESU R Free: 0.529 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 81.836 Å2
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Refinement step | Cycle: 1 / Resolution: 3.1→50 Å
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Refine LS restraints |
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