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- PDB-3n2t: Structure of the glycerol dehydrogenase AKR11B4 from Gluconobacte... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3n2t | ||||||
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Title | Structure of the glycerol dehydrogenase AKR11B4 from Gluconobacter oxydans | ||||||
![]() | Putative oxidoreductase | ||||||
![]() | OXIDOREDUCTASE / ALDO/KETO Reductase superfamily / AKR / AKR11B4 / TIM BARREL | ||||||
Function / homology | ![]() Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor / oxidoreductase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Richter, N. / Breicha, K. / Hummel, W. / Niefind, K. | ||||||
![]() | ![]() Title: The Three-Dimensional Structure of AKR11B4, a Glycerol Dehydrogenase from Gluconobacter oxydans, Reveals a Tryptophan Residue as an Accelerator of Reaction Turnover. Authors: Richter, N. / Breicha, K. / Hummel, W. / Niefind, K. #1: Journal: Chembiochem / Year: 2009 Title: Characterisation of a recombinant NADP-dependent glycerol dehydrogenase from Gluconobacter oxydans and its application in the production of L-glyceraldehyde. Authors: Richter, N. / Neumann, M. / Liese, A. / Wohlgemuth, R. / Eggert, T. / Hummel, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80 KB | Display | ![]() |
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PDB format | ![]() | 59.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.1 KB | Display | ![]() |
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Full document | ![]() | 427.9 KB | Display | |
Data in XML | ![]() | 14.9 KB | Display | |
Data in CIF | ![]() | 20.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 39076.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q5FQJ0, Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 37.56 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: protein stock solution: 10 mg/ml AKR11B4 protein, 10 mM Tris/HCl puffer, 150 mM NaCl, 0.5 mM EDTA, pH 8.5. Reservoir solution: 35 % (w/v) poly ethylen glycol 3350 (PEG 3350), 200 mM ...Details: protein stock solution: 10 mg/ml AKR11B4 protein, 10 mM Tris/HCl puffer, 150 mM NaCl, 0.5 mM EDTA, pH 8.5. Reservoir solution: 35 % (w/v) poly ethylen glycol 3350 (PEG 3350), 200 mM potassium nitrate. The crystallization drop contained equal volumes of the reservoir and the protein stock solution before equilibration. The pH-value in the crystallization drop was determined by the buffer of the protein stock solution., VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2→34.5 Å / Num. obs: 26999 / % possible obs: 99.8 % / Redundancy: 5.4 % / Biso Wilson estimate: 29.1 Å2 / Rmerge(I) obs: 0.133 / Rsym value: 0.133 / Net I/σ(I): 10.1 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.413 Å2 / ksol: 0.344 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2→24.119 Å
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Refine LS restraints |
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LS refinement shell |
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