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- PDB-5llb: Structure of Polyphosphate Kinase 2 from Francisella tularensis w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5llb | |||||||||
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Title | Structure of Polyphosphate Kinase 2 from Francisella tularensis with AMPPCH2PPP and polyphosphate | |||||||||
![]() | (Polyphosphate kinase ...) x 2 | |||||||||
![]() | TRANSFERASE / Complex with non-hydrolysable ATP analogue. Polyphosphate metabolism. Nucleotide metabolism | |||||||||
Function / homology | ![]() Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a phosphate group as acceptor / polyphosphate kinase activity / phosphorylation / 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 | ![]() | 402.6 KB | Display | ![]() |
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PDB format | ![]() | 331.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.6 MB | Display | ![]() |
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Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 45 KB | Display | |
Data in CIF | ![]() | 63.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5lc9C ![]() 5lcdC ![]() 5ld1C ![]() 5ldbC ![]() 5ll0C ![]() 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
-Polyphosphate kinase ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 32135.043 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: SCHU S4 / Schu 4 / Gene: ppk2, FTT_1564, BZ14_1190 / Production host: ![]() ![]() References: UniProt: Q5NEQ5, ATP-polyphosphate phosphotransferase #2: Protein | Mass: 31426.197 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: SCHU S4 / Schu 4 / Gene: ppk2, FTT_1564, BZ14_1190 / Production host: ![]() ![]() References: UniProt: Q5NEQ5, ATP-polyphosphate phosphotransferase |
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-Non-polymers , 5 types, 688 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/6YZ.gif)
![](data/chem/img/6YW.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/6YZ.gif)
![](data/chem/img/6YW.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CL / #4: Chemical | ChemComp-MG / #5: Chemical | ChemComp-6YZ / [[( #6: Chemical | ChemComp-6YW / [ #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.7 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: 20 % PEG 1500, pH 8 PCTP buffer, 0.5 mM polyP, 5 mM AMPPCH2P, 10 mM MgCl2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 7, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 1.92→72.46 Å / Num. obs: 82008 / % possible obs: 99.3 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 13.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3CZQ Resolution: 1.92→72.46 Å / Cross valid method: FREE R-VALUE
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Refinement step | Cycle: LAST / Resolution: 1.92→72.46 Å
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