+Open data
-Basic information
Entry | Database: PDB / ID: 2fmo | ||||||
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Title | Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase | ||||||
Components | 5,10-methylenetetrahydrofolate reductase | ||||||
Keywords | OXIDOREDUCTASE / TIM BARREL / FLAVIN / REDUCTASE | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Pejchal, R. / Campbell, E. / Guenther, B.D. / Lennon, B.W. / Matthews, R.G. / Ludwig, M.L. | ||||||
Citation | Journal: Biochemistry / Year: 2006 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fmo.cif.gz | 176.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fmo.ent.gz | 138.1 KB | Display | PDB format |
PDBx/mmJSON format | 2fmo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/2fmo ftp://data.pdbj.org/pub/pdb/validation_reports/fm/2fmo | HTTPS FTP |
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-Related structure data
Related structure data | 2fmnC 1b5tS C: citing same article (ref.) S: Starting model for refinement |
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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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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. |
-Components
#1: Protein | Mass: 34243.902 Da / Num. of mol.: 3 / Mutation: A177V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: metF / Plasmid: pET23B / Production host: Escherichia coli (E. coli) References: UniProt: P0AEZ1, methylenetetrahydrofolate reductase [NAD(P)H] #2: Chemical | ChemComp-SO4 / #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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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: 2.67 Å3/Da / Density % sol: 53.86 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG 4000, LITHIUM SULFATE, SODIUM CACODYLATE, ETHANOL, METHYLPENTANEDIOL, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 1, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→20.01 Å / Num. all: 50976 / Num. obs: 50832 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 25.1 Å2 / Rsym value: 0.048 / Net I/σ(I): 15.9 |
Reflection shell | Resolution: 2.25→2.33 Å / Rsym value: 0.297 / % possible all: 98.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 1B5T Resolution: 2.25→20.01 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2391033.06 / 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: 54.9211 Å2 / ksol: 0.367372 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.25→20.01 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.39 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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