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- PDB-1qlu: STRUCTURE OF THE H422A MUTANT VANILLYL-ALCOHOL OXIDASE IN COMPLEX... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qlu | ||||||
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Title | STRUCTURE OF THE H422A MUTANT VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL | ||||||
![]() | VANILLYL-ALCOHOL OXIDASE | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN / METHANOL UTILIZATION / PEROXISOME / FLAVOENZYME / OXIDASE / CATALYSIS | ||||||
Function / homology | ![]() vanillyl-alcohol oxidase / vanillyl-alcohol oxidase activity / methanol metabolic process / : / D-lactate dehydrogenase (cytochrome) activity / lactate catabolic process / D-lactate dehydrogenase activity / FAD binding / peroxisome / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mattevi, A. | ||||||
![]() | ![]() Title: Covalent Flavinylation is Essential for Efficient Redox Catalysis in Vanillyl-Alcohol Oxidase Authors: Fraaije, M.W. / Van Den Heuvel, R.H.H. / Van Berkel, W.J. / Mattevi, A. #1: Journal: Proteins: Struct.,Funct., Genet. / Year: 1997 Title: Crystallization and Preliminary X-Ray Analysis of the Flavoenzyme Vanillyl-Alcohol Oxidase from Penicillium Simplicissimum Authors: Mattevi, A. / Fraaije, M.W. / Coda, A. / Van Berkel, W.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 232.6 KB | Display | ![]() |
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PDB format | ![]() | 185.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 983.6 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 49 KB | Display | |
Data in CIF | ![]() | 65.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.230985, -0.972806, 0.017171), Vector: |
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Components
#1: Protein | Mass: 62939.910 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 40 % | |||||||||||||||
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Crystal grow | pH: 4.6 / Details: FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6 | |||||||||||||||
Crystal grow | *PLUS pH: 5.1 / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1998 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→30 Å / Num. obs: 43343 / % possible obs: 94.8 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Rsym value: 0.119 / Net I/σ(I): 4.9 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.321 / Mean I/σ(I) obs: 1.9 / Rsym value: 0.321 / % possible all: 88.4 |
Reflection | *PLUS Num. measured all: 216054 / Rmerge(I) obs: 0.119 |
Reflection shell | *PLUS % possible obs: 88.4 % / Mean I/σ(I) obs: 2.5 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.4→30 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.4→30 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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