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- PDB-4jeq: Different Contribution of Conserved Amino Acids to the Global Pro... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4jeq | ||||||
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Title | Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes | ||||||
![]() | TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | ||||||
![]() | ISOMERASE / TIM BARREL / DISEASE MUTATION / PENTOSE SHUNT / GLUCONEOGENESIS / GLYCOLYSIS | ||||||
Function / homology | ![]() glycosome / triose-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / gluconeogenesis / glycolytic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hernandez-Santoyo, A. / Aguirre-Fuentes, Y. / Torres-Larios, A. / Gomez-Puyou, A. / De Gomez-Puyou, M.T. | ||||||
![]() | ![]() Title: Different contribution of conserved amino acids to the global properties of triosephosphate isomerases. Authors: Aguirre, Y. / Cabrera, N. / Aguirre, B. / Perez-Montfort, R. / Hernandez-Santoyo, A. / Reyes-Vivas, H. / Enriquez-Flores, S. / de Gomez-Puyou, M.T. / Gomez-Puyou, A. / Sanchez-Ruiz, J.M. / Costas, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 555.8 KB | Display | ![]() |
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PDB format | ![]() | 462.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 546.8 KB | Display | ![]() |
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Full document | ![]() | 593.4 KB | Display | |
Data in XML | ![]() | 105.3 KB | Display | |
Data in CIF | ![]() | 146.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4hhpC ![]() 2j27S 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
#1: Protein | Mass: 26851.807 Da / Num. of mol.: 12 / Mutation: E104D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-PEG / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.69 % |
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Crystal grow | Temperature: 281.15 K / Method: vapor diffusion, sitting drop / pH: 8.6 Details: 25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K |
-Data collection
Diffraction | Mean temperature: 113 K | ||||||||||||||||||
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Diffraction source | Source: ![]() | ||||||||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 28, 2010 Details: HIGH-RESOLUTION DOUBLE- CRYSTAL SI(220) SAGITTAL FOCUSING, ROSENBAUM-ROCK VERTICAL FOCUSING MIRROR | ||||||||||||||||||
Radiation | Monochromator: ROSENBAUM-ROCK MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 2.3→89.78 Å / Num. all: 122434 / Num. obs: 122434 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3 % / Biso Wilson estimate: 36.51 Å2 / Rmerge(I) obs: 0.089 / Rsym value: 0.086 / Net I/σ(I): 8.1 | ||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2J27 Resolution: 2.303→61.577 Å / SU ML: 0.31 / σ(F): 1.34 / Phase error: 28.35 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.303→61.577 Å
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Refine LS restraints |
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LS refinement shell |
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