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Open data
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Basic information
Entry | Database: PDB / ID: 8k40 | ||||||
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Title | mercuric reductase,GbsMerA, - FAD bound | ||||||
![]() | NAD(P)/FAD-dependent oxidoreductase | ||||||
![]() | TRANSFERASE / Mercuric reductase / Gelidibacter salicanalis PAMC21136 / Hg resistance / Heavy metal detoxification | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Do, H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Biochemical and structural basis of mercuric reductase, GbsMerA, from Gelidibacter salicanalis PAMC21136. Authors: Pardhe, B.D. / Lee, M.J. / Lee, J.H. / Do, H. / Oh, T.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.8 KB | Display | ![]() |
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PDB format | ![]() | 145.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 951.8 KB | Display | ![]() |
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Full document | ![]() | 959 KB | Display | |
Data in XML | ![]() | 31.9 KB | Display | |
Data in CIF | ![]() | 43.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8k41C 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
#1: Protein | Mass: 49953.340 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.16 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop Details: 1.6 M sodium phosphate monobasic/0.4 M potassium phosphate dibasic, 0.1 M sodium phosphate dibasic/citric acid (pH 4.2)] |
-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 14, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→29.38 Å / Num. obs: 33032 / % possible obs: 99.9 % / Redundancy: 13.2 % / CC1/2: 1 / Rmerge(I) obs: 0.11 / Net I/σ(I): 15.5 |
Reflection shell | Resolution: 2.6→2.72 Å / Rmerge(I) obs: 1.6 / Num. unique obs: 3967 / CC1/2: 0.8 |
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Processing
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Refinement | Method to determine structure: ![]() 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 / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 78.656 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→29.38 Å
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Refine LS restraints |
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LS refinement shell |
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