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- PDB-2oip: Crystal Structure of the S290G Active Site Mutant of TS-DHFR from... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2oip | ||||||
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Title | Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis | ||||||
![]() | Chain A, crystal structure of Dhfr | ||||||
![]() | TRANSFERASE / OXIDOREDUCTASE / BIFUNCTIONAL ENZYME | ||||||
Function / homology | ![]() Thymidylate Synthase; Chain A / Thymidylate synthase/dCMP hydroxymethylase domain / Dihydrofolate Reductase, subunit A / Dihydrofolate Reductase, subunit A / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Martucci, W.E. / Vargo, M.A. | ||||||
![]() | ![]() Title: Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis Authors: Doan, L.T. / Martucci, W.E. / Vargo, M.A. / Atreya, C.E. / Anderson, K.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 | ![]() | 540.4 KB | Display | ![]() |
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PDB format | ![]() | 445.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 5.9 MB | Display | ![]() |
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Full document | ![]() | 6 MB | Display | |
Data in XML | ![]() | 117.9 KB | Display | |
Data in CIF | ![]() | 151.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1qzfS 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Details | The biological assembly is the dimer present in the asymmetric unit, either with monomers A+B or C+D. The second half of the dimer formed by monomer E lies across the crystallographic axis. |
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Components
-Protein , 1 types, 5 molecules ABCDE
#1: Protein | Mass: 60014.219 Da / Num. of mol.: 5 / Mutation: S290G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q5CGA3, thymidylate synthase, dihydrofolate reductase |
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-Non-polymers , 5 types, 424 molecules ![](data/chem/img/UMP.gif)
![](data/chem/img/CB3.gif)
![](data/chem/img/MTX.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CB3.gif)
![](data/chem/img/MTX.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-UMP / #3: Chemical | ChemComp-CB3 / #4: Chemical | ChemComp-MTX / #5: Chemical | ChemComp-NDP / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.49 Å3/Da / Density % sol: 72.63 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.1mM ammonium sulfate, 0.3M lithium sulfate, 0.1M Tris, 10% PEG 6000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 9, 2005 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. obs: 130177 / % possible obs: 99.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.3 % / Biso Wilson estimate: 65 Å2 / Rmerge(I) obs: 0.117 / Χ2: 1.234 / Net I/σ(I): 13.4 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.538 / Mean I/σ(I) obs: 2.9 / Num. unique all: 12987 / Χ2: 1.252 / % possible all: 99.6 |
-Phasing
Phasing dm | FOM : 0.783 / FOM centric: 0.676 / Reflection: 131011 / Reflection centric: 4636 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Phasing dm shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB Entry 1QZF Resolution: 2.8→50 Å / FOM work R set: 0.78 / Isotropic thermal model: group / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 66.525 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.98 Å / Rfactor Rfree error: 0.012
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