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- PDB-5d4j: Chloride-bound form of a copper nitrite reductase from Alcaligene... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5d4j | ||||||
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Title | Chloride-bound form of a copper nitrite reductase from Alcaligenes faecals | ||||||
![]() | Copper-containing nitrite reductase | ||||||
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Function / homology | ![]() denitrification pathway / ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fukuda, Y. / Tse, K.M. / Nakane, T. / Nakatsu, T. / Suzuki, M. / Sugahara, M. / Inoue, S. / Yumoto, F. / Matsugaki, N. / Nango, E. ...Fukuda, Y. / Tse, K.M. / Nakane, T. / Nakatsu, T. / Suzuki, M. / Sugahara, M. / Inoue, S. / Yumoto, F. / Matsugaki, N. / Nango, E. / Tono, K. / Joti, Y. / Kameshima, T. / Song, C. / Yabashi, M. / Nureki, O. / Murphy, M.E.P. / Inoue, T. / Iwata, S. / Mizohata, E. | ||||||
![]() | ![]() Title: Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography Authors: Fukuda, Y. / Tse, K.M. / Nakane, T. / Nakatsu, T. / Suzuki, M. / Sugahara, M. / Inoue, S. / Masuda, T. / Yumoto, F. / Matsugaki, N. / Nango, E. / Tono, K. / Joti, Y. / Kameshima, T. / Song, ...Authors: Fukuda, Y. / Tse, K.M. / Nakane, T. / Nakatsu, T. / Suzuki, M. / Sugahara, M. / Inoue, S. / Masuda, T. / Yumoto, F. / Matsugaki, N. / Nango, E. / Tono, K. / Joti, Y. / Kameshima, T. / Song, C. / Hatsui, T. / Yabashi, M. / Nureki, O. / Murphy, M.E. / Inoue, T. / Iwata, S. / Mizohata, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 212 KB | Display | ![]() |
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PDB format | ![]() | 166.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4yscC ![]() 4yseC ![]() 5d4hC ![]() 5d4iC ![]() 5f7aC ![]() 5f7bC C: citing same article ( |
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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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Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 37019.922 Da / Num. of mol.: 3 / Fragment: UNP residues 40-376 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 407 molecules ![](data/chem/img/CU.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CU / ![]() #3: Chemical | ![]() #4: Chemical | ChemComp-GOL / ![]() #5: Chemical | ![]() #6: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.74 % |
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.1 Details: 1:1 mixture of the purified protein solution (40 mg/ml) and a reservoir solution composed of 100 mM sodium acetate (pH 4.1) and 7% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Dec 10, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2→50 Å / Num. obs: 62159 / % possible obs: 100 % / Redundancy: 24.2 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 19.2 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 24 % / Mean I/σ(I) obs: 1.8 / % possible all: 100 |
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Processing
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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: 33.144 Å2
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Refinement step | Cycle: 1 / Resolution: 2→24.79 Å
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Refine LS restraints |
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