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Open data
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Basic information
Entry | Database: PDB / ID: 1ht0 | ||||||
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Title | HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE | ||||||
![]() | CLASS I ALCOHOL DEHYDROGENASE 3, GAMMA SUBUNIT | ||||||
![]() | OXIDOREDUCTASE / rossmann fold / alcohol dehydrogenase / zinc | ||||||
Function / homology | ![]() Ethanol oxidation / RA biosynthesis pathway / 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 / zinc ion binding ...Ethanol oxidation / RA biosynthesis pathway / 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 / zinc ion binding / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Niederhut, M.S. / Gibbons, B.J. / Perez-Miller, S. / Hurley, T.D. | ||||||
![]() | ![]() Title: Three-dimensional structures of the three human class I alcohol dehydrogenases. Authors: Niederhut, M.S. / Gibbons, B.J. / Perez-Miller, S. / 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 | ![]() | 167.3 KB | Display | ![]() |
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PDB format | ![]() | 129.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 967.3 KB | Display | ![]() |
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Full document | ![]() | 972.5 KB | Display | |
Data in XML | ![]() | 34.9 KB | Display | |
Data in CIF | ![]() | 52.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hsoC ![]() 1hszC ![]() 1dehS S: Starting model for refinement C: citing same article ( |
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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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Details | biological dimer is within the asymmetric unit |
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Components
#1: Protein | Mass: 39743.266 Da / Num. of mol.: 2 / Fragment: GAMMA SUBUNIT / Mutation: POLYMORPHIC VARIANT WITH Q271 AND V349 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45.96 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 9 Details: 100 mM Tris, 4 mM NAD+, 18% PEG 6000, 10 mg/ml protein, pH 9.0, VAPOR DIFFUSION, SITTING DROP at 277K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Aug 31, 1998 / Details: yale focusing mirrors |
Radiation | Monochromator: yale focusing mirrors with nickel filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→44 Å / Num. all: 48663 / Num. obs: 47641 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 22.2 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 21.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.216 / Mean I/σ(I) obs: 6.7 / % possible all: 86.8 |
Reflection | *PLUS Num. measured all: 188548 |
Reflection shell | *PLUS % possible obs: 86.8 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1DEH Resolution: 2→44 Å / Isotropic thermal model: isotropic individual / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 21 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→44 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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