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Open data
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Basic information
Entry | Database: PDB / ID: 1fgj | ||||||
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Title | X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE | ||||||
![]() | HYDROXYLAMINE OXIDOREDUCTASE | ||||||
![]() | OXIDOREDUCTASE / NITRIFICATION | ||||||
Function / homology | ![]() hydroxylamine dehydrogenase / hydroxylamine oxidase activity / hydroxylamine oxidase / anaerobic respiration, using ammonium as electron donor / hydroxylamine oxidoreductase activity / anammoxosome / protein homotrimerization / oxidoreductase activity / heme binding / identical protein binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tanaka, N. / Igarashi, N. / Moriyama, H. | ||||||
![]() | ![]() Title: The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Authors: Igarashi, N. / Moriyama, H. / Fujiwara, T. / Fukumori, Y. / Tanaka, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 218 KB | Display | ![]() |
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PDB format | ![]() | 186.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 27.6 KB | Display | |
Data in CIF | ![]() | 38.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 61736.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Chemical | ChemComp-HEM / #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 297 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: IMAGE PLATE / Date: May 6, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→40 Å / Num. obs: 33905 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 12.2 % / Rmerge(I) obs: 0.79 |
Reflection shell | Resolution: 2.8→2.97 Å / Redundancy: 9.5 % / Rmerge(I) obs: 0.166 / % possible all: 95 |
Reflection shell | *PLUS % possible obs: 95 % |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE AUTHORS REFINED THE STRUCTURE BY ELIMINATING THE REPULSIVE FORCES BETWEEN HEME P460 AND ADJACENT TYR 467, BECAUSE AT PRESENT, X-PLOR CANNOT CONSTRAIN THE LINKAGE BETWEEN CRYSTALLOGRAPHIC ...Details: THE AUTHORS REFINED THE STRUCTURE BY ELIMINATING THE REPULSIVE FORCES BETWEEN HEME P460 AND ADJACENT TYR 467, BECAUSE AT PRESENT, X-PLOR CANNOT CONSTRAIN THE LINKAGE BETWEEN CRYSTALLOGRAPHIC RELATED SUBUNITS. THIS UNUSUAL LINKAGE IS THOUGHT TO BE COVALENT BOND.
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Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.23 / Rfactor Rwork: 0.23 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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