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- PDB-4n4l: Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in h... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4n4l | |||||||||
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Title | Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydrazine | |||||||||
![]() | hydroxylamine oxidoreductase | |||||||||
![]() | OXIDOREDUCTASE / C-type cytochrome | |||||||||
Function / homology | ![]() hydroxylamine oxidase / anaerobic respiration, using ammonium as electron donor / hydroxylamine oxidoreductase activity / anammoxosome / protein homotrimerization / nitric oxide biosynthetic process / heme binding / identical protein binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Maalcke, W.J. / Dietl, A. / Marritt, S.J. / Butt, J.N. / Jetten, M.S.M. / Keltjens, J.T. / Barends, T.R.M.B. / Kartal, B. | |||||||||
![]() | ![]() Title: Structural Basis of Biological NO Generation by Octaheme Oxidoreductases. Authors: Maalcke, W.J. / Dietl, A. / Marritt, S.J. / Butt, J.N. / Jetten, M.S. / Keltjens, J.T. / Barends, T.R. / Kartal, B. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.6 KB | Display | ![]() |
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PDB format | ![]() | 104.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.1 MB | Display | ![]() |
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Full document | ![]() | 3.1 MB | Display | |
Data in XML | ![]() | 25 KB | Display | |
Data in CIF | ![]() | 37.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4n4jSC ![]() 4n4kC ![]() 4n4mC ![]() 4n4nC ![]() 4n4oC S: Starting model for refinement 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | Covalent trimer confirmed by SDS-PAGE, analytical ultracentrifugation, and gel filtration |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 56543.637 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q1PX48, hydroxylamine oxidase |
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-Non-polymers , 6 types, 438 molecules ![](data/chem/img/PO4.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HZN.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HG1.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HZN.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HG1.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-EDO / #4: Chemical | ChemComp-HZN / | #5: Chemical | ChemComp-HEC / #6: Chemical | ChemComp-HG1 / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 1.3 M ammonium sulfate, 0.05-0.10 M sodium phosphate, pH 7.4, detergent additive cyclohexylbutanoyl-N-hydroxyethylglucamide (C-HEGA-10), VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 1, 2011 |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→46 Å / Num. all: 54927 / Num. obs: 54927 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.1 / Net I/σ(I): 18 |
Reflection shell | Resolution: 1.9→2 Å / Rmerge(I) obs: 0.464 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4N4J Resolution: 1.9→45.96 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.958 / SU B: 1.832 / SU ML: 0.055 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.104 / ESU R Free: 0.093 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.714 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→45.96 Å
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Refine LS restraints |
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