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Open data
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Basic information
Entry | Database: PDB / ID: 1oen | ||||||
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Title | PHOSPHOENOLPYRUVATE CARBOXYKINASE | ||||||
![]() | PHOSPHOENOLPYRUVATE CARBOXYKINASE | ||||||
![]() | KINASE / P-LOOP / NUCLEOTIDE-TRIPHOSPHATE HYDROLASE | ||||||
Function / homology | ![]() phosphoenolpyruvate carboxykinase (ATP) / phosphoenolpyruvate carboxykinase (ATP) activity / gluconeogenesis / calcium ion binding / magnesium ion binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Matte, A. / Goldie, H. / Sweet, R.M. / Delbaere, L.T.J. | ||||||
![]() | ![]() 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. #1: ![]() Title: Reactivity of Cysteinyl, Arginyl, and Lysyl Residues of Escherichia Coli Phosphoenolpyruvate Carboxykinase Against Group-Specific Chemical Reagents Authors: Bazaes, S. / Silva, R. / Goldie, H. / Cardemil, E. / Jabalquinto, A.M. #2: ![]() Title: Crystallization of the Calcium-Activated Phosphoenolpyruvate Carboxykinase from Escherichia Coli K12 Authors: Delbaere, L.T. / Vandonselaar, M. / Glaeske, D. / Jabs, C. / Goldie, H. #3: ![]() 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. #4: ![]() Title: Allosteric Control by Calcium and Mechanism of Desensitization of Phosphoenolpyruvate Carboxykinase of Escherichia Coli Authors: Goldie, H. / Sanwal, B.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 112.6 KB | Display | ![]() |
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PDB format | ![]() | 87.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 379.5 KB | Display | ![]() |
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Full document | ![]() | 386.8 KB | Display | |
Data in XML | ![]() | 11.6 KB | Display | |
Data in CIF | ![]() | 18.2 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 58944.082 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: ONE MOLECULE EACH OF ACETATE AND ACETOACETATE APPEARS TO BE BOUND WITHIN THE ACTIVE SITE Source: (natural) ![]() ![]() References: UniProt: P22259, phosphoenolpyruvate carboxykinase (ATP) |
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#2: Chemical | ChemComp-ACT / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: seeding | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Jun 3, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Redundancy: 5 % / Rmerge(I) obs: 0.068 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 47596 / % possible obs: 90.8 % / Num. measured all: 249762 / Rmerge(I) obs: 0.093 |
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Processing
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Refinement | Resolution: 1.9→6 Å / σ(F): 0 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: 31.35 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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