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- PDB-1mg5: Crystal structure of Drosophila melanogaster alcohol dehydrogenas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mg5 | ||||||
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Title | Crystal structure of Drosophila melanogaster alcohol dehydrogenase complexed with NADH and acetate at 1.6 A | ||||||
![]() | alcohol dehydrogenase | ||||||
![]() | OXIDOREDUCTASE / SDR / ADH / Drosophila melanogaster / NADH / acetate | ||||||
Function / homology | ![]() alcohol catabolic process / ethanol metabolic process / acetaldehyde dehydrogenase (acetylating) activity / alcohol metabolic process / acetaldehyde metabolic process / behavioral response to ethanol / alcohol dehydrogenase (NAD+) activity / : / : / alcohol dehydrogenase ...alcohol catabolic process / ethanol metabolic process / acetaldehyde dehydrogenase (acetylating) activity / alcohol metabolic process / acetaldehyde metabolic process / behavioral response to ethanol / alcohol dehydrogenase (NAD+) activity / : / : / alcohol dehydrogenase / oxidoreductase activity / protein homodimerization activity / protein-containing complex / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Benach, J. / Atrian, S. / Gonzalez-Duarte, R. / Ladenstein, R. | ||||||
![]() | ![]() Title: Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis Authors: Benach, J. / Winberg, J.O. / Svendsen, J.S. / Atrian, S. / Gonzalez-Duarte, R. / Ladenstein, R. #1: ![]() Title: The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution Authors: Benach, J. / Atrian, S. / Gonzalez-Duarte, R. / Ladenstein, R. #2: ![]() Title: The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: Observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography Authors: Benach, J. / Atrian, S. / Gonzalez-Duarte, R. / Ladenstein, R. | ||||||
History |
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Remark 999 | sequence Since the protein was purified directly from Drosophila melanogaster ADH. The first ...sequence Since the protein was purified directly from Drosophila melanogaster ADH. The first residue: Met1 is cleaved off in the matured Drosophila melanogaster ADH-S enzyme. For this reason it is not present in the crystal structure. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 129.8 KB | Display | ![]() |
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PDB format | ![]() | 99.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 550 KB | Display | ![]() |
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Full document | ![]() | 557.7 KB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 23.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1a4uS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 27656.834 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: ADH-Slow allele / Source: (natural) ![]() ![]() #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: 2.26 Å3/Da / Density % sol: 45.68 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.1 M TRIS/HCl, 30% PEG4000, 0.2M NaAcetate trihydrate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 8.6 / Method: vapor diffusion | ||||||||||||||||||||||||||||||
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: Feb 10, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→40 Å / Num. obs: 60633 / % possible obs: 96.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.5 % / Biso Wilson estimate: 15.3 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 19.7 |
Reflection shell | Resolution: 1.63→1.68 Å / Rmerge(I) obs: 0.36 / % possible all: 73.3 |
Reflection | *PLUS Num. measured all: 438968 |
Reflection shell | *PLUS % possible obs: 73.3 % / Rmerge(I) obs: 0.36 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1a4u Resolution: 1.63→20 Å / Isotropic thermal model: isotropic / Cross valid method: free R-factor / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 14.6 Å2 | |||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.16 Å / Luzzati d res low obs: 5 Å | |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.63→20 Å
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Refine LS restraints |
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Refinement | *PLUS | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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