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- PDB-3dg8: Quadruple mutant (N51I+C59R+S108N+I164L) Plasmodium falciparum di... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3dg8 | ||||||
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Title | Quadruple mutant (N51I+C59R+S108N+I164L) Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) complexed with RJF670, NADPH, and dUMP | ||||||
![]() | (Bifunctional dihydrofolate reductase-thymidylate ...) x 2 | ||||||
![]() | OXIDOREDUCTASE / TRANSFERASE / Alpha-Beta / Methyltransferase | ||||||
Function / homology | ![]() Interconversion of nucleotide di- and triphosphates / thymidylate synthase / thymidylate synthase activity / dTMP biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / methylation / mitochondrion ...Interconversion of nucleotide di- and triphosphates / thymidylate synthase / thymidylate synthase activity / dTMP biosynthetic process / dihydrofolate reductase / dihydrofolate reductase activity / tetrahydrofolate biosynthetic process / one-carbon metabolic process / methylation / mitochondrion / RNA binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dasgupta, T. / Chitnumsub, P. / Maneeruttanarungroj, C. / Kamchonwongpaisan, S. / Nichols, S. / Lyons, T.M. / Tirado-Rives, J. / Jorgensen, W.L. / Yuthavong, Y. / Anderson, K.S. | ||||||
![]() | ![]() Title: Exploiting structural analysis, in silico screening, and serendipity to identify novel inhibitors of drug-resistant falciparum malaria. Authors: Dasgupta, T. / Chitnumsub, P. / Kamchonwongpaisan, S. / Maneeruttanarungroj, C. / Nichols, S.E. / Lyons, T.M. / Tirado-Rives, J. / Jorgensen, W.L. / Yuthavong, Y. / 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 | ![]() | 245.3 KB | Display | ![]() |
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PDB format | ![]() | 194.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 47.4 KB | Display | |
Data in CIF | ![]() | 63.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3dgaC ![]() 1j3kS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Details | The biological unit is the same as asymmetric unit. |
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Components
-Bifunctional dihydrofolate reductase-thymidylate ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 33213.309 Da / Num. of mol.: 2 / Fragment: Residues 1-280 / Mutation: N51I, C59R, S108N, I164L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: V1/S / Plasmid: pET17b / Production host: ![]() ![]() References: UniProt: Q8I1R6, UniProt: P13922*PLUS, dihydrofolate reductase, thymidylate synthase #2: Protein | Mass: 38712.949 Da / Num. of mol.: 2 / Fragment: Residues 281-608 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: V1/S / Plasmid: pET17b / Production host: ![]() ![]() References: UniProt: Q8I1R6, UniProt: P13922*PLUS, dihydrofolate reductase, thymidylate synthase |
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-Non-polymers , 4 types, 266 molecules ![](data/chem/img/RJ6.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/UMP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NDP.gif)
![](data/chem/img/UMP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Sequence details | THE SEQUENCE INFORMATIO |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 50.8 % |
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Crystal grow | Temperature: 297 K / pH: 4.6 Details: PEG 4000, NH4OAc, pH 4.6, MICROBATCH, temperature 297K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 10, 2007 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.56→50 Å / Num. obs: 45609 / % possible obs: 97.6 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 39.4 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 2.56→2.65 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.265 / Mean I/σ(I) obs: 6.36 / Rsym value: 0.265 / % possible all: 95 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1J3K Resolution: 2.58→49.43 Å / Occupancy max: 1 / Occupancy min: 1 / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Bsol: 36.44 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.26 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.58→49.43 Å
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Refine LS restraints |
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Xplor file |
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