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- PDB-3cls: Crystal structure of the R236C mutant of ETF from Methylophilus m... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3cls | ||||||
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Title | Crystal structure of the R236C mutant of ETF from Methylophilus methylotrophus | ||||||
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![]() | ELECTRON TRANSPORT / ETF / TMADH / electron transfer / dynamic interface / FAD / Flavoprotein / Transport | ||||||
Function / homology | ![]() fatty acid beta-oxidation using acyl-CoA dehydrogenase / amino acid catabolic process / flavin adenine dinucleotide binding / electron transfer activity / nucleotide binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Katona, G. / Leys, D. | ||||||
![]() | ![]() Title: Probing the dynamic interface between trimethylamine dehydrogenase (TMADH) and electron transferring flavoprotein (ETF) in the TMADH-2ETF complex: role of the Arg-alpha237 (ETF) and Tyr-442 (TMADH) residue pair. Authors: Burgess, S.G. / Messiha, H.L. / Katona, G. / Rigby, S.E. / Leys, D. / Scrutton, N.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 246.3 KB | Display | ![]() |
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PDB format | ![]() | 193.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3clrC ![]() 3cltC ![]() 3cluC ![]() 1o97S 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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Unit cell |
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Components
#1: Protein | Mass: 28929.850 Da / Num. of mol.: 1 / Mutation: R237C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: etfB / Production host: ![]() ![]() |
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#2: Protein | Mass: 33700.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: etfA / Production host: ![]() ![]() |
#3: Chemical | ChemComp-AMP / |
#4: Chemical | ChemComp-FAD / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.46 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.2 Details: limited digest with trypsin, 2.0 M sodium phosphate, pH 6.2, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Apr 1, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→20 Å / Num. all: 72327 / Num. obs: 72327 / % possible obs: 95.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rsym value: 0.084 / Net I/σ(I): 7.3 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: 1O97 Resolution: 1.65→20 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.963 / SU B: 3.461 / SU ML: 0.065 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.086 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.334 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.652→1.695 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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