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- PDB-1flg: CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1flg | |||||||||
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Title | CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA | |||||||||
![]() | PROTEIN (QUINOPROTEIN ETHANOL DEHYDROGENASE) | |||||||||
![]() | OXIDOREDUCTASE / QUINOPROTEIN / SUPERBARREL / DEHYDROGENASE | |||||||||
Function / homology | ![]() alcohol dehydrogenase (cytochrome c) activity => GO:0052934 / alcohol dehydrogenase (cytochrome c) activity => GO:0052934 / : / alcohol dehydrogenase (cytochrome c) / ethanol catabolic process / outer membrane-bounded periplasmic space / calcium ion binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Keitel, T. / Diehl, A. / Knaute, T. / Stezowski, J.J. / Hohne, W. / Gorisch, H. | |||||||||
![]() | ![]() Title: X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. Authors: Keitel, T. / Diehl, A. / Knaute, T. / Stezowski, J.J. / Hohne, W. / Gorisch, 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 | ![]() | 236.6 KB | Display | ![]() |
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PDB format | ![]() | 193.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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
#1: Protein | Mass: 64123.270 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-CA / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.7 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 10% PEG1500, 50 MM CALCIUM CHLORIDE, 4.5 MM GLYCINE/NAOH PH 8, pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Details: Stezowski, J.J., (1989) J. Mol. Biol., 205, 617. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 29, 1989 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.52→25.7 Å / Num. obs: 41300 / % possible obs: 94.2 % / Observed criterion σ(I): 1 / Redundancy: 2.7 % / Biso Wilson estimate: 28.2 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.6→2.7 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.33 / % possible all: 98.8 |
Reflection | *PLUS Highest resolution: 2.52 Å / Lowest resolution: 25.7 Å / Observed criterion σ(I): 1 / Redundancy: 2.7 % / Num. measured all: 109117 / Rmerge(I) obs: 0.126 / Biso Wilson estimate: 28.2 Å2 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.7 Å / Rmerge(I) obs: 0.36 |
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Processing
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Refinement | Resolution: 2.6→12.5 Å / σ(F): 1 / σ(I): 1 / Details: MAXIMUM LIKELIHOOD
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Refinement step | Cycle: LAST / Resolution: 2.6→12.5 Å
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Refine LS restraints | Type: p_bond_d / Dev ideal: 0.013 | |||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.192 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 28.2 Å2 | |||||||||||||||||||||
Refine LS restraints | *PLUS
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