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- PDB-1e47: L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73Q -
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Open data
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Basic information
Entry | Database: PDB / ID: 1.0E+47 | |||||||||
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Title | L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73Q | |||||||||
![]() | L-FUCULOSE 1-PHOSPHATE ALDOLASE | |||||||||
![]() | ALDOLASE (CLASS II) / BACTERIAL L-FUCOSE METABOLISM / CLEAVAGE OF L-FUCULOSE 1-PHOSPHATE TO DIHYDROXYACETONE PHOSPHATE AND L-LACTALDEHYDE / MUTANT STRUCTURE | |||||||||
Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Joerger, A.C. / Schulz, G.E. | |||||||||
![]() | ![]() Title: Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis. Authors: Joerger, A.C. / Mueller-Dieckmann, C. / Schulz, G.E. #1: ![]() Title: Catalytic Action of Fuculose 1-Phosphate Aldolase (Class II) as Derived by Structure-Directed Mutagenesis Authors: Joerger, A.C. / Gosse, C. / Fessner, W.-D. / Schulz, G.E. #2: ![]() Title: Catalytic Mechanism of the Metal-Dependent Fuculose Aldolase from Escherichia Coli as Derived from the Structure Authors: Dreyer, M.K. / Schulz, G.E. #3: Journal: J.Mol.Biol. / Year: 1993 Title: The Spatial Structure of the Class II L-Fuculose-1-Phosphate Aldolase from Escherichia Coli Authors: Dreyer, M.K. / Schulz, G.E. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.3 KB | Display | ![]() |
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PDB format | ![]() | 41.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1e46C ![]() 1e48C ![]() 1e49C ![]() 1e4aC ![]() 1e4bC ![]() 1e4cC 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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Unit cell |
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Details | BIOMOLECULE |
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Components
-Protein , 1 types, 1 molecules P
#1: Protein | Mass: 23804.334 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Description: E73Q MUTATION PERFORMED WITH PHOSPHOROTHIOATE METHOD USING M13MP19 Plasmid: PKKFA2-E73Q / Production host: ![]() ![]() ![]() References: UniProt: P11550, UniProt: P0AB87*PLUS, ![]() |
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-Non-polymers , 5 types, 122 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/13P.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/13P.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ![]() #3: Chemical | ChemComp-BME / | ![]() #4: Chemical | ChemComp-13P / | ![]() #5: Chemical | ChemComp-ZN / | #6: Water | ChemComp-HOH / | ![]() |
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-Details
Compound details | CHAIN P ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 39 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion, hanging drop / pH: 8 Details: CRYSTALS GROWN FROM AMMONIUM SULFATE AT PH 8.0, VAPOUR DIFFUSION, HANGING DROP, CONDITIONS CLOSE TO THE ONES REPORTED FOR THE WILD-TYPE, SEE PDB ID 1FUA FOR FURTHER DETAILS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 7.6 / Method: vapor diffusion, hanging dropDetails: Dreyer, M.K., (1996) Acta Crystallog. sect., D52, 1082. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MULTIWIRE SIEMENS X-100 / Detector: AREA DETECTOR / Date: Jul 15, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.15→10 Å / Num. obs: 10320 / % possible obs: 95 % / Redundancy: 3.4 % / Rsym value: 0.044 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.15→2.22 Å / Redundancy: 2.1 % / Mean I/σ(I) obs: 6 / Rsym value: 0.13 / % possible all: 87 |
Reflection | *PLUS Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS % possible obs: 87 % / Num. unique obs: 861 / Rmerge(I) obs: 0.13 |
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Processing
Software |
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Refinement | Method to determine structure![]() Details: THE 9 C-TERMINAL RESIDUES (LYS207 - GLU 215) WERE NOT SEEN IN THE DENSITY MAPS
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Displacement parameters | Biso mean: 27.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→10 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.15 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |