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- PDB-1djq: STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF RECOMBINANT C30A M... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1djq | ||||||
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Title | STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF RECOMBINANT C30A MUTANT OF TRIMETHYLAMINE DEHYDROGENASE FROM METHYLOPHILUS METHYLOTROPHUS (SP. W3A1) | ||||||
![]() | TRIMETHYLAMINE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE / IRON-SULFUR FLAVOPROTEIN / ELECTRON TRANSFER | ||||||
Function / homology | ![]() trimethylamine dehydrogenase / trimethylamine dehydrogenase activity / fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway / 2,4-dienoyl-CoA reductase (NADPH) activity / FMN binding / 4 iron, 4 sulfur cluster binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Trickey, P. / Basran, J. / Lian, L.-Y. / Chen, Z.-W. / Barton, J.D. / Sutcliffe, M.J. / Scrutton, N.S. / Mathews, F.S. | ||||||
![]() | ![]() Title: Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)). Authors: Trickey, P. / Basran, J. / Lian, L.Y. / Chen, Z. / Barton, J.D. / Sutcliffe, M.J. / Scrutton, N.S. / Mathews, F.S. #1: ![]() Title: Correlation of X-Ray Deduced and Experimental Amino Acid Sequences of Trimethylamine Dehydrogenase Authors: Barber, M.J. / Neame, P.J. / Lim, L.W. / White, S. / Mathews, F.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 309.4 KB | Display | ![]() |
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PDB format | ![]() | 247.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 56.7 KB | Display | |
Data in CIF | ![]() | 81.5 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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1 |
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Unit cell |
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Details | The biological assembly is a dimer related by a molecular 2-fold axis. |
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Components
#1: Protein | Mass: 81573.961 Da / Num. of mol.: 2 / Mutation: C30A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: W3A1 / Plasmid: PKK223-3 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.62 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop, microseeding / pH: 6.5 Details: PEG 8000, phosphate buffer, sodium chloride, pH 6.5, vapor diffusion,hanging drop and microseeding, temperature 295.0K |
Crystal grow | *PLUS Method: vapor diffusion, hanging drop |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Nov 21, 1995 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.22→10 Å / Num. all: 86826 / Num. obs: 81611 / % possible obs: 93.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 18.6 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 22.2 |
Reflection shell | Resolution: 2.22→2.32 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.123 / Num. unique all: 17184 / % possible all: 71.7 |
Reflection | *PLUS Lowest resolution: 50 Å |
Reflection shell | *PLUS % possible obs: 71.7 % / Mean I/σ(I) obs: 6.4 |
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Processing
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Refinement | Resolution: 2.2→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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