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- PDB-4o9u: Mechanism of transhydrogenase coupling proton translocation and h... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4o9u | ||||||
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Title | Mechanism of transhydrogenase coupling proton translocation and hydride transfer | ||||||
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![]() | MEMBRANE PROTEIN / Nicotinamide nucleotide transhydrogenase / Couples proton motive / Hydride transfer / Holo-transhydrogease from Thermus thermophilus assembled from subunits alpha1 / alpha2 / truncated beta / and domain III as a dimer / Respiratory proton pump enzyme forming cytosolic NADP(H) / Protons and NAD(H) / NADP(H) / Proton translocation and hydride transfer / Periplasmic membrane and cytosol | ||||||
Function / homology | ![]() : / proton-translocating NAD(P)+ transhydrogenase activity / proton-translocating NAD(P)+ transhydrogenase / NADPH regeneration / NADP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Leung, J.H. / Yamaguchi, M. / Moeller, A. / Schurig-Briccio, L.A. / Gennis, R.B. / Potter, C.S. / Carragher, B. / Stout, C.D. | ||||||
![]() | ![]() Title: Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Authors: Leung, J.H. / Schurig-Briccio, L.A. / Yamaguchi, M. / Moeller, A. / Speir, J.A. / Gennis, R.B. / Stout, C.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 | ![]() | 346.7 KB | Display | ![]() |
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PDB format | ![]() | 283.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 66.8 KB | Display | |
Data in CIF | ![]() | 88 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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Unit cell |
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Components
#1: Protein | Mass: 10649.571 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 47371.906 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein | Mass: 41258.828 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Chemical | #5: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.93 Å3/Da / Density % sol: 68.7 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 50 mM MgCl2, 0.5 M trimethylamine N-oxide, 26% polyethylenglycol 400, 2% octyl glucoside, 0.1mM NADP, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD |
Radiation | Monochromator: Side scattering I-beam bent single crystal; asymmetric cut 4.9650 deg. Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.12709 Å / Relative weight: 1 |
Reflection | Resolution: 6.926→38.9 Å / Num. all: 5015 / Num. obs: 4922 / % possible obs: 98.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 160.054 Å2
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Refinement step | Cycle: LAST / Resolution: 6.926→38.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 6.926→7.105 Å / Total num. of bins used: 20
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