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Open data
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Basic information
Entry | Database: PDB / ID: 1e0u | ||||||
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Title | Structure R271L mutant of E. coli pyruvate kinase | ||||||
![]() | Pyruvate kinase | ||||||
![]() | PHOSPHOTRANSFERASE / GLYCOLYSIS / ALLOSTERY | ||||||
Function / homology | ![]() pyruvate kinase complex / pyruvate kinase / pyruvate kinase activity / potassium ion binding / phosphorylation / glycolytic process / kinase activity / response to heat / magnesium ion binding / ATP binding ...pyruvate kinase complex / pyruvate kinase / pyruvate kinase activity / potassium ion binding / phosphorylation / glycolytic process / kinase activity / response to heat / magnesium ion binding / ATP binding / identical protein binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fortin, R. / Mattevi, A. | ||||||
![]() | ![]() Title: The Allosteric Regulation of Pyruvate Kinase. Authors: Valentini, G. / Chiarelli, L. / Fortin, R. / Speranza, M.L. / Galizzi, A. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 355.8 KB | Display | ![]() |
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PDB format | ![]() | 283.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1e0tC ![]() 1pkyS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 50751.352 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: pykF, AC789_1c18560, ACN002_1349, EL75_1979, EL79_2019, EL80_2048, HMPREF3040_05259 Production host: ![]() ![]() References: UniProt: A0A0A0G552, UniProt: P0AD61*PLUS, pyruvate kinase #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | Compound details | CHAIN A, B, C, D ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 56.93 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.2 / Details: pH 6.20 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 1997 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→15 Å / Num. obs: 56604 / % possible obs: 97.7 % / Redundancy: 2.7 % / Rmerge(I) obs: 0.09 / Rsym value: 0.09 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 2 % / Rmerge(I) obs: 0.201 / Mean I/σ(I) obs: 3.1 / Rsym value: 0.201 / % possible all: 86.1 |
Reflection | *PLUS Num. measured all: 151954 |
Reflection shell | *PLUS % possible obs: 86.1 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PKY Resolution: 2.8→15 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.8→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_plane_restr / Dev ideal: 0.009 |