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- PDB-1d1t: MUTANT OF HUMAN SIGMA ALCOHOL DEHYDROGENASE WITH LEUCINE AT POSIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1d1t | ||||||
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Title | MUTANT OF HUMAN SIGMA ALCOHOL DEHYDROGENASE WITH LEUCINE AT POSITION 141 | ||||||
![]() | ALCOHOL DEHYDROGENASE CLASS IV SIGMA CHAIN | ||||||
![]() | OXIDOREDUCTASE / ROSSMANN OR DINUCLEOTIDE FOLD | ||||||
Function / homology | ![]() omega-hydroxydecanoate dehydrogenase / omega-hydroxydecanoate dehydrogenase activity / ethanol binding / aldehyde oxidase activity / all-trans-retinol dehydrogenase (NAD+) / fatty acid omega-oxidation / receptor antagonist activity / Ethanol oxidation / alcohol dehydrogenase (NAD+) activity / alcohol dehydrogenase (NAD+) activity, zinc-dependent ...omega-hydroxydecanoate dehydrogenase / omega-hydroxydecanoate dehydrogenase activity / ethanol binding / aldehyde oxidase activity / all-trans-retinol dehydrogenase (NAD+) / fatty acid omega-oxidation / receptor antagonist activity / Ethanol oxidation / alcohol dehydrogenase (NAD+) activity / alcohol dehydrogenase (NAD+) activity, zinc-dependent / : / all-trans-retinol dehydrogenase (NAD+) activity / alcohol dehydrogenase / retinol metabolic process / retinoic acid metabolic process / retinoid metabolic process / retinol binding / response to bacterium / response to ethanol / zinc ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Xie, P.T. / Hurley, T.D. | ||||||
![]() | ![]() Title: Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase. Authors: Xie, P.T. / Hurley, T.D. #1: ![]() Title: X-ray structure of human class IV sigma-sigma alcohol dehydrogenase Authors: Xie, P.T. / Parsons, S.H. / Speckhard, D.C. / Bosron, W.F. / Hurley, T.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 301.5 KB | Display | ![]() |
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PDB format | ![]() | 244.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 60.9 KB | Display | |
Data in CIF | ![]() | 82 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 39906.312 Da / Num. of mol.: 4 / Mutation: M141L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 412 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/NAD.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/NAD.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-ACT / #4: Chemical | ChemComp-CAC / #5: Chemical | ChemComp-NAD / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.25 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 100 mM Cacodylate, pH 6.5, 100 mM Zinc Acetate, 7.5 mM NAD+, 18% PEG 6000, 8 mg/ml enzyme, VAPOR DIFFUSION, SITTING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Sep 14, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. all: 70587 / Num. obs: 64234 / % possible obs: 91 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.67 % / Biso Wilson estimate: 45 Å2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 2.4→2.51 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.403 / Num. unique all: 8552 / % possible all: 77 |
Reflection | *PLUS Num. measured all: 171372 |
Reflection shell | *PLUS % possible obs: 77 % / Mean I/σ(I) obs: 2.1 |
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Processing
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Refinement | Resolution: 2.4→50 Å / σ(F): 0.5 / σ(I): 0.5 / Stereochemistry target values: Engh and Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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