+Open data
-Basic information
Entry | Database: PDB / ID: 6qu0 | ||||||
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Title | Structure of azoreductase from Bacillus sp. A01 | ||||||
Components | FMN-dependent NADH-azoreductase | ||||||
Keywords | OXIDOREDUCTASE / Flavoprotein Oxidoreductase FMN Azoreductase Azo dyes | ||||||
Function / homology | Function and homology information FMN-dependent NADH-azoreductase / oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor / oxidoreductase activity, acting on other nitrogenous compounds as donors / FMN binding / electron transfer activity Similarity search - Function | ||||||
Biological species | Bacillus okhensis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Savino, S. / Fraaije, M.W. | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2020 Title: Mechanistic and Crystallographic Studies of Azoreductase AzoA fromBacillus wakoensisA01. Authors: Romero, E. / Savino, S. / Fraaije, M.W. / Loncar, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6qu0.cif.gz | 100.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6qu0.ent.gz | 76.9 KB | Display | PDB format |
PDBx/mmJSON format | 6qu0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/6qu0 ftp://data.pdbj.org/pub/pdb/validation_reports/qu/6qu0 | HTTPS FTP |
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-Related structure data
Related structure data | 3w7aS S: Starting model for refinement |
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Similar structure data | |
Experimental dataset #1 | Data reference: 10.18430/m36qu0 / Data set type: diffraction image data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 23553.732 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus okhensis (bacteria) / Gene: azoR, LQ50_08590 / Production host: Escherichia coli (E. coli) References: UniProt: A0A0B0IKH9, Oxidoreductases; Acting on other nitrogenous compounds as donors #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-SO4 / | #5: Water | ChemComp-HOH / | |
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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: 2.4 Å3/Da / Density % sol: 48.75 % |
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Crystal grow | Temperature: 294.15 K / Method: vapor diffusion, hanging drop / Details: 0.15M ammonium sulfate 25% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.54179 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 28, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 |
Reflection | Resolution: 1.79→42.92 Å / Num. obs: 43095 / % possible obs: 99 % / Redundancy: 6.8 % / Net I/σ(I): 8.4 |
Reflection shell | Resolution: 1.79→1.83 Å |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3W7A Resolution: 1.8→42.96 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.947 / SU B: 3.883 / SU ML: 0.112 / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.126 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.947 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→42.96 Å
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Refine LS restraints |
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