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- PDB-1a72: AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE L... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1a72 | ||||||
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Title | AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD | ||||||
![]() | HORSE LIVER ALCOHOL DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE / OXIDOREDUCTASE (NAD(A)-CHOH(D)) / ACTIVE SITE MUTANT / LIVER ALCOHOL DEHYDROGENASE / ISOSTERIC NAD INHIBITORS | ||||||
Function / homology | ![]() : / : / all-trans-retinol dehydrogenase (NAD+) activity / alcohol dehydrogenase / retinol metabolic process / retinoic acid metabolic process / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Colby, T.D. / Bahnson, B.J. / Chin, J.K. / Klinman, J.P. / Goldstein, B.M. | ||||||
![]() | ![]() Title: Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes. Authors: Colby, T.D. / Bahnson, B.J. / Chin, J.K. / Klinman, J.P. / Goldstein, B.M. #1: ![]() Title: A Link between Protein Structure and Enzyme Catalyzed Hydrogen Tunneling Authors: Bahnson, B.J. / Colby, T.D. / Chin, J.K. / Goldstein, B.M. / Klinman, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.4 KB | Display | ![]() |
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PDB format | ![]() | 63.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 700.6 KB | Display | ![]() |
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Full document | ![]() | 714.4 KB | Display | |
Data in XML | ![]() | 18.2 KB | Display | |
Data in CIF | ![]() | 24.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1a71C ![]() 8adhS 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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Components
#1: Protein | Mass: 39864.258 Da / Num. of mol.: 1 / Mutation: F93W, V203A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-PAD / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.82 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.4 Details: CRYSTALS GROWN FROM 4 MICROLITER HANGING DROPS OF 10MG/ML PROTEIN IN 50 MM TRIS BUFFER (PH8.4 @4C) 4% (V/V) ETOH EQUILIBRATED AT 4C WITH WELLS CONTAINING 11-13% ETOH, vapor diffusion - ...Details: CRYSTALS GROWN FROM 4 MICROLITER HANGING DROPS OF 10MG/ML PROTEIN IN 50 MM TRIS BUFFER (PH8.4 @4C) 4% (V/V) ETOH EQUILIBRATED AT 4C WITH WELLS CONTAINING 11-13% ETOH, vapor diffusion - hanging drop, temperature 277K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 275 K |
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Diffraction source | Source: ![]() |
Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: Dec 15, 1993 |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→22 Å / Num. obs: 10388 / % possible obs: 76.9 % / Observed criterion σ(I): 2 / Biso Wilson estimate: 38 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.56→2.68 Å / Mean I/σ(I) obs: 2 / % possible all: 43 |
Reflection | *PLUS Num. measured all: 16939 / Rmerge(I) obs: 0.078 |
Reflection shell | *PLUS % possible obs: 43 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 8ADH Resolution: 2.6→8 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: A POSTERIORI / σ(F): 2 Details: RFREE FIGURE BELONGS TO SA OMIT PROCEDURE USED TO CONFIRM FIT OF LIGAND. THIS RFREE DESCRIBES A MODEL NOT CONTAINING SOLVENT
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Displacement parameters | Biso mean: 16.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.36 Å / Luzzati d res low obs: 5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.71 Å / Rfactor Rfree error: 0.04 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.234 |