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- PDB-1igw: Crystal Structure of the Isocitrate Lyase from the A219C mutant o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1igw | |||||||||
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Title | Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli | |||||||||
![]() | Isocitrate lyase | |||||||||
![]() | LYASE / BETA BARREL | |||||||||
Function / homology | ![]() isocitrate lyase / cation binding / isocitrate lyase activity / glyoxylate cycle / tricarboxylic acid cycle / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Britton, K.L. / Abeysinghe, I.S.B. / Baker, P.J. / Barynin, V. / Diehl, P. / Langridge, S.J. / McFadden, B.A. / Sedelnikova, S.E. / Stillman, T.J. / Weeradechapon, K. / Rice, D.W. | |||||||||
![]() | ![]() Title: The structure and domain organization of Escherichia coli isocitrate lyase. Authors: Britton, K.L. / Abeysinghe, I.S. / Baker, P.J. / Barynin, V. / Diehl, P. / Langridge, S.J. / McFadden, B.A. / Sedelnikova, S.E. / Stillman, T.J. / Weeradechapon, K. / Rice, D.W. #1: ![]() Title: Use of Chemical Modification in the Crystallization of Isocitrate Lyase from Escherichia coli Authors: Abeysinghe, S.I. / Baker, P.J. / Rice, D.W. / Rodgers, H.F. / Stillman, T.J. / Ko, Y.H. / McFadden, B.A. / Nimmo, H.G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 340.2 KB | Display | ![]() |
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PDB format | ![]() | 274.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 474 KB | Display | ![]() |
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Full document | ![]() | 517.1 KB | Display | |
Data in XML | ![]() | 70.7 KB | Display | |
Data in CIF | ![]() | 98.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Details | The given tetramer defines the biological assembly |
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Components
#1: Protein | Mass: 47598.395 Da / Num. of mol.: 4 / Mutation: A219C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-HG / #3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-PYR / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.21 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7 Details: MEPEG 2000, magnesium chloride, ethyl mercury thiosalicylate, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 19, 1995 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→33.3 Å / Num. all: 188246 / Num. obs: 96329 / % possible obs: 94.1 % / Redundancy: 2 % / Rmerge(I) obs: 0.051 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.216 / Num. unique all: 6893 / % possible all: 91.3 |
Reflection | *PLUS Num. measured all: 188246 |
Reflection shell | *PLUS % possible obs: 91.3 % / Num. unique obs: 6893 / Num. measured obs: 13435 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 31 Å2 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Rfactor obs: 0.184 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 31 Å2 | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.297 / Rfactor obs: 0.234 |