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Yorodumi- PDB-4b63: A. fumigatus ornithine hydroxylase (SidA) bound to NADP and ornithine -
+Open data
-Basic information
Entry | Database: PDB / ID: 4b63 | ||||||
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Title | A. fumigatus ornithine hydroxylase (SidA) bound to NADP and ornithine | ||||||
Components | L-ORNITHINE N5 MONOOXYGENASE | ||||||
Keywords | OXIDOREDUCTASE / SIDEROPHORE / FLAVIN | ||||||
Function / homology | Function and homology information L-ornithine N5-monooxygenase [NAD(P)H] / ferrichrome biosynthetic process / ornithine N5-monooxygenase activity / siderophore-dependent iron import into cell / ergosterol biosynthetic process / cellular response to iron ion starvation / N,N-dimethylaniline monooxygenase activity / siderophore biosynthetic process / secondary metabolite biosynthetic process / NADP+ binding ...L-ornithine N5-monooxygenase [NAD(P)H] / ferrichrome biosynthetic process / ornithine N5-monooxygenase activity / siderophore-dependent iron import into cell / ergosterol biosynthetic process / cellular response to iron ion starvation / N,N-dimethylaniline monooxygenase activity / siderophore biosynthetic process / secondary metabolite biosynthetic process / NADP+ binding / monooxygenase activity / intracellular iron ion homeostasis / iron ion binding Similarity search - Function | ||||||
Biological species | ASPERGILLUS FUMIGATUS (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Franceschini, S. / Fedkenheuer, M. / Vogelaar, N.J. / Robinson, H.H. / Sobrado, P. / Mattevi, A. | ||||||
Citation | Journal: Biochemistry / Year: 2012 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4b63.cif.gz | 198.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4b63.ent.gz | 156.4 KB | Display | PDB format |
PDBx/mmJSON format | 4b63.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b6/4b63 ftp://data.pdbj.org/pub/pdb/validation_reports/b6/4b63 | HTTPS FTP |
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-Related structure data
Related structure data | 4b64C 4b65C 4b66C 4b67C 4b68C 4b69C 3s61S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-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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-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.) ASPERGILLUS FUMIGATUS (mold) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q5SE95, UniProt: E9QYP0*PLUS |
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-Non-polymers , 6 types, 270 molecules
#2: Chemical | ChemComp-FAD / | ||
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#3: Chemical | ChemComp-NAP / | ||
#4: Chemical | ChemComp-ORN / | ||
#5: Chemical | ChemComp-SO4 / | ||
#6: Chemical | ChemComp-GOL / #7: Water | ChemComp-HOH / | |
-Details
Sequence details | GENBANK ENTRY GB AAT84594.1 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.09 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: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 35689 / % possible obs: 98.7 % / Redundancy: 13.8 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 13 % / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 5.1 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3S61 Resolution: 1.9→42.21 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.934 / SU B: 5.181 / SU ML: 0.088 / Cross valid method: THROUGHOUT / ESU R: 0.175 / ESU R Free: 0.148 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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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: 33.593 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→42.21 Å
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