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Open data
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Basic information
Entry | Database: PDB / ID: 3ge8 | ||||||
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Title | Toluene 4-monooxygenase HD T201A diferric, resting state complex | ||||||
![]() | (Toluene-4-monooxygenase system protein ...) x 4 | ||||||
![]() | OXIDOREDUCTASE / DIIRON HYDROXYLASE / EFFECTOR PROTEIN / T4MOH / T201A / Aromatic hydrocarbons catabolism / FAD / Flavoprotein / Iron / Monooxygenase | ||||||
Function / homology | ![]() toluene 4-monooxygenase / toluene 4-monooxygenase activity / toluene catabolic process / monooxygenase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Elsen, N.L. / Bailey, L.J. / Hauser, A.D. / Fox, B.G. | ||||||
![]() | ![]() Title: Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Authors: Elsen, N.L. / Bailey, L.J. / Hauser, A.D. / Fox, B.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 439.3 KB | Display | ![]() |
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PDB format | ![]() | 350.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 496.7 KB | Display | ![]() |
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Full document | ![]() | 524.4 KB | Display | |
Data in XML | ![]() | 86.3 KB | Display | |
Data in CIF | ![]() | 125.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3ge3C ![]() 3dhhS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Toluene-4-monooxygenase system protein ... , 4 types, 8 molecules ADBFCGEH
#1: Protein | Mass: 58139.312 Da / Num. of mol.: 2 / Mutation: T201A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q6Q8Q7, UniProt: Q00456*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of ...References: UniProt: Q6Q8Q7, UniProt: Q00456*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor #2: Protein | Mass: 38433.262 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00460, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor #3: Protein | Mass: 9600.989 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00457, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor #4: Protein | Mass: 11629.032 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00459, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
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-Non-polymers , 3 types, 1449 molecules ![](data/chem/img/FE.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-FE / #6: Chemical | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.63 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 25% PEG 3350, 200 mM Na Acetate, 100 mM Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Apr 17, 2008 |
Radiation | Monochromator: Diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97926 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→50 Å / Num. all: 115810 / Num. obs: 108513 / % possible obs: 93.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Highest resolution: 2.19 Å / % possible all: 99.65 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3DHH Resolution: 2.19→47.17 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.916 / SU B: 4.779 / SU ML: 0.126 / Cross valid method: THROUGHOUT / ESU R: 0.264 / ESU R Free: 0.211 / 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: 17.187 Å2
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Refinement step | Cycle: LAST / Resolution: 2.19→47.17 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.188→2.244 Å / Total num. of bins used: 20
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