+Open data
-Basic information
Entry | Database: PDB / ID: 1t9g | ||||||
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Title | Structure of the human MCAD:ETF complex | ||||||
Components |
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Keywords | oxidoreductase / electron transport / electron transfer / protein:protein complex / fatty acid oxidation / human electron transferring flavoprotein / human medium chain acyl coa dehydrogenase | ||||||
Function / homology | Function and homology information electron transfer flavoprotein complex / medium-chain fatty acid catabolic process / mitochondrial fatty acid beta-oxidation of unsaturated fatty acids / carnitine metabolic process, CoA-linked / medium-chain acyl-CoA dehydrogenase / Beta oxidation of octanoyl-CoA to hexanoyl-CoA / Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA / medium-chain fatty acyl-CoA dehydrogenase activity / carnitine biosynthetic process / fatty acid beta-oxidation using acyl-CoA dehydrogenase ...electron transfer flavoprotein complex / medium-chain fatty acid catabolic process / mitochondrial fatty acid beta-oxidation of unsaturated fatty acids / carnitine metabolic process, CoA-linked / medium-chain acyl-CoA dehydrogenase / Beta oxidation of octanoyl-CoA to hexanoyl-CoA / Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA / medium-chain fatty acyl-CoA dehydrogenase activity / carnitine biosynthetic process / fatty acid beta-oxidation using acyl-CoA dehydrogenase / medium-chain fatty acid metabolic process / acyl-CoA dehydrogenase activity / amino acid catabolic process / Respiratory electron transport / cardiac muscle cell differentiation / glycogen biosynthetic process / regulation of gluconeogenesis / fatty acid beta-oxidation / response to starvation / Protein methylation / respiratory electron transport chain / response to cold / post-embryonic development / liver development / mitochondrial membrane / PPARA activates gene expression / flavin adenine dinucleotide binding / electron transfer activity / oxidoreductase activity / mitochondrial matrix / axon / mitochondrion / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Toogood, H.S. / van Thiel, A. / Basran, J. / Sutcliffe, M.J. / Scrutton, N.S. / Leys, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain Acyl-CoA dehydrogenase complex Authors: Toogood, H.S. / van Thiel, A. / Basran, J. / Sutcliffe, M.J. / Scrutton, N.S. / Leys, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t9g.cif.gz | 375.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t9g.ent.gz | 303.4 KB | Display | PDB format |
PDBx/mmJSON format | 1t9g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t9/1t9g ftp://data.pdbj.org/pub/pdb/validation_reports/t9/1t9g | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 43695.812 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACADM / Production host: Escherichia coli (E. coli) / References: UniProt: P11310, EC: 1.3.99.3 #2: Protein | | Mass: 35121.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ETFA / Production host: Escherichia coli (E. coli) / References: UniProt: P13804 #3: Protein | | Mass: 27885.646 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ETFB / Production host: Escherichia coli (E. coli) / References: UniProt: P38117 #4: Chemical | ChemComp-FAD / #5: Chemical | ChemComp-AMP / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.98 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 10-15% PEG 2000 MME, 0.2 M KSCN, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Mar 12, 2003 |
Radiation | Monochromator: diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→20 Å / Num. obs: 51756 / % possible obs: 98.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.118 / Net I/σ(I): 13.2 |
Reflection shell | Resolution: 2.9→3 Å / Mean I/σ(I) obs: 2.9 / Rsym value: 0.387 / % possible all: 84.9 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→20 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.877 / SU B: 16.828 / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R Free: 0.429 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.434 Å2
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Refinement step | Cycle: LAST / Resolution: 2.9→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→2.974 Å / Total num. of bins used: 20 /
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