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Open data
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Basic information
Entry | Database: PDB / ID: 1u2g | ||||||
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Title | transhydrogenase (dI.ADPr)2(dIII.NADPH)1 asymmetric complex | ||||||
![]() | (NAD(P) transhydrogenase subunit ...) x 2 | ||||||
![]() | OXIDOREDUCTASE / NAD(P) transhydrogenase subunits / NAD+ / NADP+ | ||||||
Function / homology | ![]() NAD(P)+ transhydrogenase (Si-specific) activity / proton-translocating NAD(P)+ transhydrogenase activity / proton-translocating NAD(P)+ transhydrogenase / NADPH regeneration / NADH binding / NAD+ binding / NAD binding / NADP binding / membrane => GO:0016020 / protein dimerization activity / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mather, O.C. / Singh, A. / van Boxel, G.I. / White, S.A. / Jackson, J.B. | ||||||
![]() | ![]() Title: Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Authors: Mather, O.C. / Singh, A. / van Boxel, G.I. / White, S.A. / Jackson, J.B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 186.7 KB | Display | ![]() |
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PDB format | ![]() | 146.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 591.6 KB | Display | ![]() |
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Full document | ![]() | 600.7 KB | Display | |
Data in XML | ![]() | 19.8 KB | Display | |
Data in CIF | ![]() | 29.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1u28C ![]() 1u2dC ![]() 1u31C ![]() 1hzzS 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
-NAD(P) transhydrogenase subunit ... , 2 types, 3 molecules ABC
#1: Protein | Mass: 40324.785 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q60164, UniProt: Q2RSB2*PLUS, EC: 1.6.1.2 #2: Protein | | Mass: 21485.510 Da / Num. of mol.: 1 / Fragment: Residues 262-464 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q59765, UniProt: Q2RSB4*PLUS, EC: 1.6.1.2 |
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-Non-polymers , 4 types, 179 molecules ![](data/chem/img/APR.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | ChemComp-GOL / | #5: Chemical | ChemComp-NDP / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.08 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: ammonium sulphate, PEG, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→46 Å / Num. all: 55412 / Num. obs: 55412 / % possible obs: 100 % / Redundancy: 4.2 % / Rsym value: 0.046 / Net I/σ(I): 17 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1hzz Resolution: 2.2→46 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→46 Å
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Refine LS restraints |
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