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- PDB-4bk1: Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lip... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4bk1 | ||||||
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Title | Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid- assisted flavoprotein strategy for regioselective aromatic hydroxylation: H213S mutant in complex with 3-hydroxybenzoate | ||||||
![]() | PROBABLE SALICYLATE MONOOXYGENASE | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN / GENTISATE / HYDROXYLASE / MONOOXYGENASE / PHOSPHOLIPID | ||||||
Function / homology | ![]() salicylate 1-monooxygenase / salicylate 1-monooxygenase activity / metabolic process / FAD binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Orru, R. / Montersino, S. / Barendregt, A. / Westphal, A.H. / van Duijn, E. / Mattevi, A. / van Berkel, W.J.H. | ||||||
![]() | ![]() Title: Crystal Structure of 3-Hydroxybenzoate 6-Hydroxylase Uncovers Lipid-Assisted Flavoprotein Strategy for Regioselective Aromatic Hydroxylation Authors: Montersino, S. / Orru, R. / Barendregt, A. / Westphal, A.H. / Van Duijn, E. / Mattevi, A. / Van Berkel, W.J.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 178.3 KB | Display | ![]() |
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PDB format | ![]() | 139.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 32.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bjySC ![]() 4bjzC ![]() 4bk2C ![]() 4bk3C 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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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 46897.176 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q0SFK6, salicylate 1-monooxygenase, EC: 1.14.13.24 |
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-Non-polymers , 5 types, 374 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/P3A.gif)
![](data/chem/img/3HB.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/P3A.gif)
![](data/chem/img/3HB.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-FAD / |
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#3: Chemical | ChemComp-P3A / |
#4: Chemical | ChemComp-3HB / |
#5: Chemical | ChemComp-CL / |
#6: Water | ChemComp-HOH / |
-Details
Sequence details | PRESENCE OF 6XHIS TAG AT C-TERM |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.22 % / Description: NONE |
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Crystal grow | pH: 8.5 Details: 30% PEG 4000, 0.2 M LISO4 AND 0.1 M TRIS/HCL (PH 8.5) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 26, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 1.73→44.91 Å / Num. obs: 40940 / % possible obs: 97.6 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 1.73→1.76 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 4.6 / % possible all: 99.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4BJY Resolution: 1.73→84.91 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.944 / SU B: 4.046 / SU ML: 0.07 / Cross valid method: THROUGHOUT / ESU R: 0.106 / ESU R Free: 0.108 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 192-198 ARE DISORDERED.
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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: 27.274 Å2
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Refinement step | Cycle: LAST / Resolution: 1.73→84.91 Å
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Refine LS restraints |
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