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- PDB-7p8l: Crystal structure of Pyrococcus abyssi 8-oxoguanine DNA glycosyla... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7p8l | ||||||
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Title | Crystal structure of Pyrococcus abyssi 8-oxoguanine DNA glycosylase (PabAGOG) in complex with dsDNA containing cytosine opposite to 8-oxoG | ||||||
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![]() | HYDROLASE / 8-oxoguanine DNA glycosylase / Pyrococcus abyssi / protein-DNA complex | ||||||
Function / homology | ![]() oxidized base lesion DNA N-glycosylase activity / Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA-(apurinic or apyrimidinic site) lyase / base-excision repair Similarity search - Function | ||||||
Biological species | ![]() ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Coste, F. / Flament, D. / Castaing, B. | ||||||
![]() | ![]() Title: Structural and functional determinants of the archaeal 8-oxoguanine-DNA glycosylase AGOG for DNA damage recognition and processing. Authors: Franck, C. / Stephane, G. / Julien, C. / Virginie, G. / Martine, G. / Norbert, G. / Fabrice, C. / Didier, F. / Josef, S.M. / Bertrand, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 166.1 KB | Display | ![]() |
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PDB format | ![]() | 105.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.7 KB | Display | ![]() |
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Full document | ![]() | 447.6 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 22.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7olbC ![]() 7oliC ![]() 7ou3C ![]() 7oueC ![]() 7oy7SC ![]() 7p0wC ![]() 7p9zC S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 27981.463 Da / Num. of mol.: 1 / Mutation: K142Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: GE5 / Orsay / Gene: PYRAB10170, PAB1695 / Production host: ![]() ![]() References: UniProt: Q9UZY0, Hydrolases; Glycosylases; Hydrolysing N-glycosyl compounds, DNA-(apurinic or apyrimidinic site) lyase | ||||
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#2: DNA chain | Mass: 2718.780 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | ||||
#3: DNA chain | Mass: 2765.878 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | ||||
#4: Chemical | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.24 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: Na acetate pH 4.5, KCl, MPD |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Jul 2, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98011 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→46.17 Å / Num. obs: 83399 / % possible obs: 99.9 % / Redundancy: 13 % / Biso Wilson estimate: 13.07 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.046 / Net I/σ(I): 28.5 |
Reflection shell | Resolution: 1.25→1.27 Å / Rmerge(I) obs: 0.354 / Mean I/σ(I) obs: 5.3 / Num. unique obs: 4101 / CC1/2: 0.958 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 7OY7 Resolution: 1.25→46.17 Å / SU ML: 0.087 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 12.8376 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.95 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.25→46.17 Å
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Refine LS restraints |
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LS refinement shell |
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