+Open data
-Basic information
Entry | Database: PDB / ID: 1e0u | ||||||
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Title | Structure R271L mutant of E. coli pyruvate kinase | ||||||
Components | Pyruvate kinase | ||||||
Keywords | PHOSPHOTRANSFERASE / GLYCOLYSIS / ALLOSTERY | ||||||
Function / homology | Function and homology information pyruvate kinase complex / pyruvate kinase / pyruvate kinase activity / potassium ion binding / glycolytic process / cellular response to insulin stimulus / kinase activity / response to heat / phosphorylation / magnesium ion binding ...pyruvate kinase complex / pyruvate kinase / pyruvate kinase activity / potassium ion binding / glycolytic process / cellular response to insulin stimulus / kinase activity / response to heat / phosphorylation / magnesium ion binding / ATP binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Fortin, R. / Mattevi, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e0u.cif.gz | 355.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e0u.ent.gz | 283.6 KB | Display | PDB format |
PDBx/mmJSON format | 1e0u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e0u_validation.pdf.gz | 471.8 KB | Display | wwPDB validaton report |
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Full document | 1e0u_full_validation.pdf.gz | 622.7 KB | Display | |
Data in XML | 1e0u_validation.xml.gz | 84.3 KB | Display | |
Data in CIF | 1e0u_validation.cif.gz | 111.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e0/1e0u ftp://data.pdbj.org/pub/pdb/validation_reports/e0/1e0u | HTTPS FTP |
-Related structure data
Related structure data | 1e0tC 1pkyS S: Starting model for refinement C: citing same article (ref.) |
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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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-Components
#1: Protein | Mass: 50751.352 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: pykF, AC789_1c18560, ACN002_1349, EL75_1979, EL79_2019, EL80_2048, HMPREF3040_05259 Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 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: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 |
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 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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 |