+Open data
-Basic information
Entry | Database: PDB / ID: 2a1u | ||||||
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Title | Crystal structure of the human ETF E165betaA mutant | ||||||
Components |
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Keywords | ELECTRON TRANSPORT / electron transfer / mobile domain / conformational sampling | ||||||
Function / homology | Function and homology information electron transfer flavoprotein complex / fatty acid beta-oxidation using acyl-CoA dehydrogenase / Respiratory electron transport / amino acid catabolic process / Protein methylation / respiratory electron transport chain / flavin adenine dinucleotide binding / electron transfer activity / oxidoreductase activity / mitochondrial matrix / mitochondrion Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.11 Å | ||||||
Authors | Toogood, H.S. / Van Thiel, A. / Scrutton, N.S. / Leys, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Stabilization of Non-productive Conformations Underpins Rapid Electron Transfer to Electron-transferring Flavoprotein Authors: Toogood, H.S. / van Thiel, A. / 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 | 2a1u.cif.gz | 126.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2a1u.ent.gz | 95.4 KB | Display | PDB format |
PDBx/mmJSON format | 2a1u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2a1u_validation.pdf.gz | 1014.7 KB | Display | wwPDB validaton report |
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Full document | 2a1u_full_validation.pdf.gz | 1020.9 KB | Display | |
Data in XML | 2a1u_validation.xml.gz | 25 KB | Display | |
Data in CIF | 2a1u_validation.cif.gz | 35.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/2a1u ftp://data.pdbj.org/pub/pdb/validation_reports/a1/2a1u | HTTPS FTP |
-Related structure data
Related structure data | 2a1tC 1efvS S: Starting model for refinement C: citing same article (ref.) |
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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: 35121.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pK18 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P13804 |
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#2: Protein | Mass: 27827.611 Da / Num. of mol.: 1 / Mutation: E165betaA Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pK18 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P38117 |
#3: Chemical | ChemComp-FAD / |
#4: Chemical | ChemComp-AMP / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 34 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: PEG2000MME, 0.1 magnesium sulphate, 0.1M cacodylic acid, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.8123 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 5, 2005 |
Radiation | Monochromator: diamond / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8123 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 28046 / Num. obs: 28046 / % possible obs: 91 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 2.1→2.16 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.266 / Mean I/σ(I) obs: 3.4 / % possible all: 62.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1EFV Resolution: 2.11→18.74 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.902 / SU B: 5.696 / SU ML: 0.151 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.283 / ESU R Free: 0.219 / 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: 21.891 Å2
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Refinement step | Cycle: LAST / Resolution: 2.11→18.74 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.11→2.164 Å / Total num. of bins used: 20
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