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- PDB-2fmn: Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase c... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2fmn | ||||||
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Title | Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase complex with LY309887 | ||||||
![]() | 5,10-methylenetetrahydrofolate reductase | ||||||
![]() | OXIDOREDUCTASE / TIM BARREL / FLAVIN / REDUCTASE | ||||||
Function / homology | ![]() methylenetetrahydrofolate reductase (NADH) / methylenetetrahydrofolate reductase (NADH) activity / methylenetetrahydrofolate reductase (NAD(P)H) activity / methionine biosynthetic process / tetrahydrofolate interconversion / FAD binding / protein-folding chaperone binding / protein-containing complex / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Pejchal, R. / Campbell, E. / Guenther, B.D. / Lennon, B.W. / Matthews, R.G. / Ludwig, M.L. | ||||||
![]() | ![]() Title: Structural Perturbations in the Ala -> Val Polymorphism of Methylenetetrahydrofolate Reductase: How Binding of Folates May Protect against Inactivation Authors: Pejchal, R. / Campbell, E. / Guenther, B.D. / Lennon, B.W. / Matthews, R.G. / Ludwig, M.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 186.2 KB | Display | ![]() |
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PDB format | ![]() | 147.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2fmoC ![]() 1b5tS C: citing same article ( 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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1 | ![]()
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Unit cell |
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Details | This entry contains the crystallographic asymmetric unit, which consists of 3 chains. The second part of the biological assembly contains a symmetry related chain B generated by the two fold axis: -x, y, -z. The biological assembly consists of chains A, B, B', and C, where B' is the symmetry related chain B. |
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Components
#1: Protein | Mass: 34243.902 Da / Num. of mol.: 3 / Mutation: A177V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0AEZ1, methylenetetrahydrofolate reductase [NAD(P)H] #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.39 % |
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Crystal grow | Temperature: 295 K / pH: 6.5 Details: PEG 8000, MAGNESIUM ACETATE, SODIUM CACODYLATE, GLYCEROL, METHYLPENTANEDIOL, LY309887, VAPOR DIFFUSION, HANGING DROP, temperature 295K, pH 6.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jan 1, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→35.8 Å / Num. obs: 62268 / % possible obs: 93.3 % / Observed criterion σ(I): 0 / Biso Wilson estimate: 22.5 Å2 |
Reflection shell | Resolution: 2.05→2.18 Å / % possible all: 85.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1B5T Resolution: 2.05→35.78 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 547514.57 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 42.29 Å2 / ksol: 0.34 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.05→35.78 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.05→2.18 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Xplor file |
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