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Open data
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Basic information
Entry | Database: PDB / ID: 1ayl | ||||||
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Title | PHOSPHOENOLPYRUVATE CARBOXYKINASE | ||||||
![]() | PHOSPHOENOLPYRUVATE CARBOXYKINASE![]() | ||||||
![]() | KINASE (TRANSPHOSPHORYLATING) / ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Tari, L.W. / Pugazenthi, U. / Goldie, H. / Delbaere, L.T.J. | ||||||
![]() | ![]() Title: Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase. Authors: Tari, L.W. / Matte, A. / Pugazhenthi, U. / Goldie, H. / Delbaere, L.T. #1: ![]() Title: Allosteric Control by Calcium and Mechanism of Desensitization of Phosphoenolpyruvate Carboxykinase of Escherichia Coli Authors: Goldie, H. / Sanwal, B.D. #2: ![]() Title: Crystal Structure of Escherichia Coli Phosphoenolpyruvate Carboxykinase: A New Structural Family with the P-Loop Nucleoside Triphosphate Hydrolase Fold Authors: Matte, A. / Goldie, H. / Sweet, R.M. / Delbaere, L.T. #3: ![]() Title: Crystallization of the Calcium-Activated Phosphoenolpyruvate Carboxykinase from Escherichia Coli K12 Authors: Delbaere, L.T. / Vandonselaar, M. / Glaeske, D. / Jabs, C. / Goldie, H. #4: ![]() Title: Sequence of the Pcka Gene of Escherichia Coli K-12: Relevance to Genetic and Allosteric Regulation and Homology of E. Coli Phosphoenolpyruvate Carboxykinase with the Enzymes from Trypanosoma ...Title: Sequence of the Pcka Gene of Escherichia Coli K-12: Relevance to Genetic and Allosteric Regulation and Homology of E. Coli Phosphoenolpyruvate Carboxykinase with the Enzymes from Trypanosoma Brucei and Saccharomyces Cerevisiae Authors: Medina, V. / Pontarollo, R. / Glaeske, D. / Tabel, H. / Goldie, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 150.7 KB | Display | ![]() |
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PDB format | ![]() | 123.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 326 KB | Display | ![]() |
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Full document | ![]() | 335.5 KB | Display | |
Data in XML | ![]() | 13.7 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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Components
#1: Protein | ![]() Mass: 59796.254 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: ORDERED MAGNESIUM ION OBSERVED BOUND TO ATP / Source: (natural) ![]() ![]() ![]() References: UniProt: P22259, ![]() |
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#2: Chemical | ChemComp-OXL / ![]() |
#3: Chemical | ChemComp-MG / |
#4: Chemical | ChemComp-ATP / ![]() |
#5: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow![]() | *PLUS Temperature: 21 ℃ / pH: 4.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: FUJI / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Num. obs: 40067 / % possible obs: 76.7 % / Observed criterion σ(I): 1 / Redundancy: 2.2 % / Rmerge(I) obs: 0.076 |
Reflection | *PLUS Highest resolution: 1.8 Å |
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Processing
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Refinement | Resolution: 1.8→6 Å / σ(F): 2 Details: MET 477 HAS DISALLOWED RAMACHANDRAN ANGLES; THE DEPOSITORS ACCOUNT FOR THIS AS IT IS THE SECOND RESIDUE WITHIN A GAMMA-TURN.
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Displacement parameters | Biso mean: 21.42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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