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- PDB-4b66: A. fumigatus ornithine hydroxylase (SidA), reduced state bound to... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4b66 | ||||||
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Title | A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP and Arg | ||||||
![]() | L-ORNITHINE N5 MONOOXYGENASE | ||||||
![]() | OXIDOREDUCTASE / SIDEROPHORE / FLAVIN | ||||||
Function / homology | ![]() L-ornithine N5-monooxygenase [NAD(P)H] / ferrichrome biosynthetic process / ornithine N5-monooxygenase activity / siderophore-dependent iron import into cell / cellular response to iron ion starvation / siderophore biosynthetic process / N,N-dimethylaniline monooxygenase activity / ergosterol biosynthetic process / NADP+ binding / secondary metabolite biosynthetic process ...L-ornithine N5-monooxygenase [NAD(P)H] / ferrichrome biosynthetic process / ornithine N5-monooxygenase activity / siderophore-dependent iron import into cell / cellular response to iron ion starvation / siderophore biosynthetic process / N,N-dimethylaniline monooxygenase activity / ergosterol biosynthetic process / NADP+ binding / secondary metabolite biosynthetic process / monooxygenase activity / intracellular iron ion homeostasis / iron ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Franceschini, S. / Fedkenheuer, M. / Vogelaar, N.J. / Robinson, H.H. / Sobrado, P. / Mattevi, A. | ||||||
![]() | ![]() Title: Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases. Authors: Franceschini, S. / Fedkenheuer, M. / Vogelaar, N.J. / Robinson, H.H. / Sobrado, P. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 194.8 KB | Display | ![]() |
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PDB format | ![]() | 154.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 980.1 KB | Display | ![]() |
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Full document | ![]() | 990.8 KB | Display | |
Data in XML | ![]() | 20.3 KB | Display | |
Data in CIF | ![]() | 27.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4b63SC ![]() 4b64C ![]() 4b65C ![]() 4b67C ![]() 4b68C ![]() 4b69C 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 56959.680 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 6 types, 77 molecules ![](data/chem/img/ARG.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ARG / | ||||
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#3: Chemical | ChemComp-FAD / | ||||
#4: Chemical | ChemComp-NAP / | ||||
#5: Chemical | #6: Chemical | ChemComp-GOL / #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 45 % / Description: NONE |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.6 Details: HANGING DROP VAPOR DIFFUSION METHOD, WITH A RESERVOIR SOLUTION CONTAINING; 1.6 M AMMONIUM SULFATE, 0.1 M HEPES, 2% DIOXANE, PH 6.6. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→50 Å / Num. obs: 10567 / % possible obs: 96.3 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 4.5 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.7 / % possible all: 94.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4B63 Resolution: 2.9→45.07 Å / Cor.coef. Fo:Fc: 0.915 / Cor.coef. Fo:Fc free: 0.805 / SU B: 20.365 / SU ML: 0.226 / Cross valid method: THROUGHOUT / ESU R Free: 0.547 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED.
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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: 27.99 Å2
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Refinement step | Cycle: LAST / Resolution: 2.9→45.07 Å
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Refine LS restraints |
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