+Open data
-Basic information
Entry | Database: PDB / ID: 1kq7 | ||||||
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Title | E315Q Mutant Form of Fumarase C from E.coli | ||||||
Components | FUMARATE HYDRATASE CLASS II | ||||||
Keywords | LYASE / fumarate lyase | ||||||
Function / homology | Function and homology information tricarboxylic acid cycle heteromeric enzyme complex / fumarate hydratase activity / fumarate hydratase / fumarate metabolic process / malate metabolic process / tricarboxylic acid cycle / response to oxidative stress / identical protein binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Weaver, T.M. / Estevez, M. / Skarda, J. / Spencer, J. | ||||||
Citation | Journal: Protein Sci. / Year: 2002 Title: X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Authors: Estevez, M. / Skarda, J. / Spencer, J. / Banaszak, L. / Weaver, T.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kq7.cif.gz | 176.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kq7.ent.gz | 141.7 KB | Display | PDB format |
PDBx/mmJSON format | 1kq7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kq/1kq7 ftp://data.pdbj.org/pub/pdb/validation_reports/kq/1kq7 | HTTPS FTP |
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-Related structure data
Related structure data | 1fuoS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The second dimer is generated by application of the following rotation matrix 1.00x 0.00y 0.00z 207.96 0.00x 1.00y 0.00z 0.7685 0.00x 0.00y -1.00z 131.2386 |
-Components
#1: Protein | Mass: 50547.785 Da / Num. of mol.: 2 / Mutation: Glu 315 to Glutamine Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: fumc / Plasmid: pASK40 / Species (production host): Escherichia coli / Production host: Escherichia coli K12 (bacteria) / Strain (production host): K12 / References: UniProt: P05042, fumarate hydratase #2: Chemical | ChemComp-MLT / | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.57 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 3350, citrate dithiothreitol, pH 6.0, VAPOR DIFFUSION, HANGING DROP at 291K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.6 / Method: microdialysis | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: Aug 10, 1998 |
Radiation | Monochromator: graphite crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→11.5 Å / Num. all: 22978 / Num. obs: 24817 / % possible obs: 92.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 5.8 % / Biso Wilson estimate: 16.05 Å2 / Rmerge(I) obs: 0.1121 / Rsym value: 0.1819 / Net I/σ(I): 5.046 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 13 Å / % possible obs: 93.5 % / Rmerge(I) obs: 0.112 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB Entry 1fuo Resolution: 2.6→8 Å / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.71 Å /
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Refinement | *PLUS Highest resolution: 2.6 Å / Rfactor all: 0.179 / Rfactor Rfree: 0.251 / Rfactor Rwork: 0.179 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.329 / Rfactor Rwork: 0.235 |