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- PDB-4ywi: F96S/L167V Double mutant of Plasmodium Falciparum Triosephosphate... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ywi | ||||||
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Title | F96S/L167V Double mutant of Plasmodium Falciparum Triosephosphate Isomerase | ||||||
![]() | Triosephosphate isomerase | ||||||
![]() | ISOMERASE / TIM BARRELS / BETA-ALPHA BARRELS / GLYCOLYSIS | ||||||
Function / homology | ![]() triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / gluconeogenesis / glycolytic process / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Pareek, V. / Balaram, P. / Murthy, M.R.N. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme Authors: Pareek, V. / Samanta, M. / Joshi, N.V. / Balaram, H. / Murthy, M.R.N. / Balaram, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 119.1 KB | Display | ![]() |
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PDB format | ![]() | 90.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464.7 KB | Display | ![]() |
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Full document | ![]() | 467.4 KB | Display | |
Data in XML | ![]() | 23.8 KB | Display | |
Data in CIF | ![]() | 35.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4x22C ![]() 4ymzC ![]() 4yxgC ![]() 4z0jC ![]() 4z0sC ![]() 1m7pS 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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 27923.613 Da / Num. of mol.: 2 / Mutation: F96S,A163V,L167V Source method: isolated from a genetically manipulated source Details: MUTATION OF A163V PRESENT IN THE WILD TYPE TIM CONSIDERED AS TEMPLATE Source: (gene. exp.) ![]() ![]() Gene: TPI / Plasmid: pTrc99A / Details (production host): PARC1008 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.82 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 1450 22%, HEPES, Li2SO4 10mM, DTT 0.5mM, NaN3 0.5mM, EDTA 0.5mM |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 30, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→50.93 Å / Num. obs: 35109 / % possible obs: 83.6 % / Redundancy: 2.3 % / Biso Wilson estimate: 30.5 Å2 / Rmerge(I) obs: 0.076 / Net I/σ(I): 38 |
Reflection shell | Resolution: 1.85→1.94 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 12.8 / % possible all: 61.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1M7P Resolution: 1.85→33.89 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.944 / SU B: 2.6 / SU ML: 0.079 / Cross valid method: FREE R-VALUE / ESU R: 0.036 / ESU R Free: 0.031 / 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: 20 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→33.89 Å
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Refine LS restraints |
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