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- PDB-1n9g: Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n9g | ||||||
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Title | Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis | ||||||
![]() | (2,4-dienoyl-CoA reductase) x 2 | ||||||
![]() | HYDROLASE / heterodimer / Rossmann fold | ||||||
Function / homology | ![]() trans-2-enoyl-CoA reductase (NADPH) activity / enoyl-[acyl-carrier-protein] reductase (NADPH) / enoyl-[acyl-carrier-protein] reductase (NADPH) activity / fatty acid metabolic process / fatty acid biosynthetic process / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Torkko, J.M. / Koivuranta, K.T. / Kastaniotis, A.J. / Airenne, T.T. / Glumoff, T. / Ilves, M. / Hartig, A. / Gurvitz, A. / Hiltunen, J.K. | ||||||
![]() | ![]() Title: Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers. Authors: Torkko, J.M. / Koivuranta, K.T. / Kastaniotis, A.J. / Airenne, T.T. / Glumoff, T. / Ilves, M. / Hartig, A. / Gurvitz, A. / Hiltunen, J.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 453 KB | Display | ![]() |
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PDB format | ![]() | 368.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 43.9 KB | Display | |
Data in CIF | ![]() | 73 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gu7S S: Starting model for refinement |
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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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Details | There are six chains in the asymmetric unit, three of which are Etr1p protein and three are Etr2p protein. The chains form all three possible dimers: Etr1p/Etr1p homodimer, Etr2p/Etr2p homodimer and Etr1p/Etr2p heterodimer. In each dimer one chain binds NADPH and one not. |
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Components
#1: Protein | Mass: 42158.516 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 42202.531 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.89 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: ammonium sulfate, ADA/NaOH, NADPH, octanoyl-CoA, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 28, 2002 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.076 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.98 Å / Num. obs: 212894 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.98→2.086 Å |
Reflection | *PLUS Lowest resolution: 19.43 Å / % possible obs: 97.5 % / Rmerge(I) obs: 0.051 |
Reflection shell | *PLUS % possible obs: 95.2 % / Rmerge(I) obs: 0.348 / Mean I/σ(I) obs: 3.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GU7 Resolution: 1.98→19.43 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.98→19.43 Å
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Refinement | *PLUS Num. reflection obs: 202400 / Num. reflection Rfree: 10494 / Rfactor Rfree: 0.2348 / Rfactor Rwork: 0.1953 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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