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- PDB-5ll0: Structure of Polyphosphate Kinase 2 from Francisella tularensis S... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ll0 | ||||||
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Title | Structure of Polyphosphate Kinase 2 from Francisella tularensis SCHU S4 with polyphosphate | ||||||
![]() | Polyphosphate kinase 2 | ||||||
![]() | TRANSFERASE / Polyphosphate metabolism and nucleotide metabolism / Polyphosphate Kinase 2 enzyme | ||||||
Function / homology | ![]() phosphorus metabolic process / Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a phosphate group as acceptor / polyphosphate kinase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Roach, P.L. / Parnell, A.E. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures. Authors: Parnell, A.E. / Mordhorst, S. / Kemper, F. / Giurrandino, M. / Prince, J.P. / Schwarzer, N.J. / Hofer, A. / Wohlwend, D. / Jessen, H.J. / Gerhardt, S. / Einsle, O. / Oyston, P.C.F. / Andexer, J.N. / Roach, P.L. #1: ![]() Title: Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis. Authors: Batten, L.E. / Parnell, A.E. / Wells, N.J. / Murch, A.L. / Oyston, P.C. / Roach, P.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 395.6 KB | Display | ![]() |
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PDB format | ![]() | 328.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5lc9C ![]() 5lcdC ![]() 5ld1C ![]() 5ldbC ![]() 5llbC ![]() 5llfC ![]() 5maqC ![]() 5o6kC ![]() 5o6mC ![]() 3czqS 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: 32135.043 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Polyphosphate: Nine phosphates Source: (gene. exp.) ![]() Gene: ppk2, FTT_1564, BZ14_1190 / Production host: ![]() ![]() References: UniProt: Q5NEQ5, ATP-polyphosphate phosphotransferase #2: Chemical | ChemComp-9PI / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.66 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: 5 % Glycerol/PEG 4000, 0.1 M MES/imidazole pH 6.5, 0.15 M Morpheus alcohols, 1 mM polyP, 5 mM MgCl2 |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 13, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92001 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→72.81 Å / Num. obs: 76026 / % possible obs: 97.1 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 11.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3czq Resolution: 1.96→59.142 Å / Cross valid method: FREE R-VALUE
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Solvent computation | VDW probe radii: 1.11 Å | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.96→59.142 Å
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