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- PDB-2vou: Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacte... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vou | ||||||
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Title | Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacter nicotinovorans | ||||||
![]() | 2,6-DIHYDROXYPYRIDINE HYDROXYLASE | ||||||
![]() | OXIDOREDUCTASE / AROMATIC HYDROXYLASE / NICOTINE DEGRADATION / FLAVIN MONO-OXYGENASE / FAD-DEPENDENT HYDROXYLASE | ||||||
Function / homology | ![]() 2,6-dihydroxypyridine 3-monooxygenase / 2,6-dihydroxypyridine 3-monooxygenase activity / nicotine catabolic process / FAD binding / flavin adenine dinucleotide binding / protein homodimerization activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Treiber, N. / Schulz, G.E. | ||||||
![]() | ![]() Title: Structure of 2,6-Dihydroxypyridine 3-Hydroxylase from a Nicotine-Degrading Pathway. Authors: Treiber, N. / Schulz, G.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 | ![]() | 239.7 KB | Display | ![]() |
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PDB format | ![]() | 194.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 48.1 KB | Display | |
Data in CIF | ![]() | 66.4 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.5075, -0.79698, 0.32751), Vector: |
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Components
#1: Protein | Mass: 43429.449 Da / Num. of mol.: 3 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q93NG3, 2,6-dihydroxypyridine 3-monooxygenase #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, CYS 323 TO SER ENGINEERED RESIDUE IN CHAIN B, CYS 323 TO SER ...ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.02 Å3/Da / Density % sol: 69 % / Description: NONE |
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Crystal grow | pH: 6.6 Details: 0.1 M SODIUM CACODYLATE PH 6.6, 15% (W/V) PEG 8000, 200 MM MAGNESIUM ACETATE, 20% (V/V) GLYCEROL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 5, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0008 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. obs: 64088 / % possible obs: 99.7 % / Observed criterion σ(I): 2.4 / Redundancy: 4.9 % / Biso Wilson estimate: 66.3 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.6→2.8 Å / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 2.4 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.6→27.92 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.942 / SU B: 18.65 / SU ML: 0.202 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.318 / ESU R Free: 0.232 / 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: 67.04 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→27.92 Å
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Refine LS restraints |
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