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Yorodumi- PDB-1egc: STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA D... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1egc | ||||||
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Title | STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA | ||||||
Components | MEDIUM CHAIN ACYL-COA DEHYDROGENASE | ||||||
Keywords | ELECTRON TRANSFER / ACYL-COA DEHYDROGENASE / FLAVOPROTEIN | ||||||
Function / homology | Function and homology information 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 ...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 / cardiac muscle cell differentiation / glycogen biosynthetic process / regulation of gluconeogenesis / fatty acid beta-oxidation / response to starvation / response to cold / post-embryonic development / liver development / mitochondrial membrane / PPARA activates gene expression / flavin adenine dinucleotide binding / mitochondrial matrix / axon / mitochondrion / nucleus / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Lee, H.J. / Wang, M. / Paschke, R. / Nandy, A. / Ghisla, S. / Kim, J.P. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Authors: Lee, H.J. / Wang, M. / Paschke, R. / Nandy, A. / Ghisla, S. / Kim, J.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1egc.cif.gz | 310.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1egc.ent.gz | 254.1 KB | Display | PDB format |
PDBx/mmJSON format | 1egc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/1egc ftp://data.pdbj.org/pub/pdb/validation_reports/eg/1egc | HTTPS FTP |
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-Related 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: 43651.762 Da / Num. of mol.: 4 / Mutation: T255E, E376G Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH OCTANOYL-COA / Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P11310, EC: 1.3.99.3 #2: Chemical | ChemComp-CO8 / #3: Chemical | ChemComp-FAD / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Mar 8, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 51243 / % possible obs: 70.7 % / Observed criterion σ(I): 1 / Redundancy: 2.7 % / Rmerge(I) obs: 0.101 |
Reflection | *PLUS Highest resolution: 2.6 Å / Num. measured all: 137635 / Rmerge(I) obs: 0.1018 |
-Processing
Software |
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Refinement | Resolution: 2.6→10 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 16.16 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 16.162 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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