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- PDB-6h4g: Regulatory subunit of a cAMP-independent protein kinase A from Tr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6h4g | |||||||||
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Title | Regulatory subunit of a cAMP-independent protein kinase A from Trypanosoma brucei: E311A, T318R, V319A mutant bound to cAMP in the A site | |||||||||
![]() | Protein kinase A regulatory subunit | |||||||||
![]() | SIGNALING PROTEIN / Protein kinase A / Regulatory Subunit / Nucleoside-binding protein | |||||||||
Function / homology | ![]() modulation of formation of structure involved in a symbiotic process / cilium movement involved in cell motility / cAMP-dependent protein kinase regulator activity / cAMP-dependent protein kinase complex / cilium / kinase activity / intracellular signal transduction / protein phosphorylation Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Volpato Santos, Y. / Lorentzen, E. / Basquin, J. / Boshart, M. | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Purine nucleosides replace cAMP in allosteric regulation of PKA in trypanosomatid pathogens. Authors: Ober, V.T. / Githure, G.B. / Volpato Santos, Y. / Becker, S. / Moya Munoz, G. / Basquin, J. / Schwede, F. / Lorentzen, E. / Boshart, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 289.6 KB | Display | ![]() |
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PDB format | ![]() | 193.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 26.2 KB | Display | |
Data in CIF | ![]() | 36.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6floSC ![]() 6hyiC 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34383.027 Da / Num. of mol.: 2 / Mutation: E311A, T318R, V319A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: Tb11.02.2210 Production host: ![]() ![]() References: UniProt: Q385V6 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.09 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 50 mM Tris pH 8.0 0.2 mM Magnesium Chloride 40% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 19, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.144→30.21 Å / Num. obs: 31343 / % possible obs: 100 % / Redundancy: 1 % / Biso Wilson estimate: 17.8216436493 Å2 / Rpim(I) all: 0.0888 / Net I/σ(I): 0.92 |
Reflection shell | Resolution: 2.144→2.24 Å / Rpim(I) all: 0.1223 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6FLO Resolution: 2.14351698698→30.205523826 Å / SU ML: 0.380726826369 / Cross valid method: FREE R-VALUE / σ(F): 1.34684365027 / Phase error: 31.9468288459
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.8229744064 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.14351698698→30.205523826 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -20.3825618882 Å / Origin y: -12.350172076 Å / Origin z: 23.2982273412 Å
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Refinement TLS group | Selection details: all |