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Open data
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Basic information
Entry | Database: PDB / ID: 7dxq | ||||||
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Title | Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC | ||||||
![]() | Circadian clock protein kinase KaiC | ||||||
![]() | TRANSFERASE / clock protein | ||||||
Function / homology | ![]() regulation of phosphorelay signal transduction system / negative regulation of circadian rhythm / entrainment of circadian clock / protein serine/threonine/tyrosine kinase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / circadian rhythm / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity ...regulation of phosphorelay signal transduction system / negative regulation of circadian rhythm / entrainment of circadian clock / protein serine/threonine/tyrosine kinase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / circadian rhythm / non-specific serine/threonine protein kinase / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / regulation of DNA-templated transcription / magnesium ion binding / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Furuike, Y. / Akiyama, S. | ||||||
![]() | ![]() Title: Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria. Authors: Furuike, Y. / Mukaiyama, A. / Ouyang, D. / Ito-Miwa, K. / Simon, D. / Yamashita, E. / Kondo, T. / Akiyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 531.1 KB | Display | ![]() |
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PDB format | ![]() | 426.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.5 MB | Display | ![]() |
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Full document | ![]() | 3.6 MB | Display | |
Data in XML | ![]() | 105.7 KB | Display | |
Data in CIF | ![]() | 138.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7dy2C ![]() 7dyiC ![]() 7dyjC ![]() 7dykC ![]() 7v3xC ![]() 2gblS S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 58232.727 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: PCC 7942 / FACHB-805 / Gene: kaiC, Synpcc7942_1216, see0011 / Plasmid: pGEX-6P-1 / Production host: ![]() ![]() References: UniProt: Q79PF4, non-specific serine/threonine protein kinase #2: Chemical | ChemComp-ATP / #3: Chemical | ChemComp-MG / #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.86 % |
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Crystal grow | Temperature: 313 K / Method: evaporation / pH: 5 / Details: Acetatic acid, Sodium formate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: May 30, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 75955 / % possible obs: 99.9 % / Redundancy: 7.4 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 21.4 |
Reflection shell | Resolution: 2.8→2.9 Å / Num. unique obs: 7451 / CC1/2: 0.751 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2GBL Resolution: 2.8→29.96 Å / Cor.coef. Fo:Fc: 0.886 / Cor.coef. Fo:Fc free: 0.814 / SU B: 22.673 / SU ML: 0.441 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.545 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 105.83 Å2 / Biso mean: 39.961 Å2 / Biso min: 3.93 Å2
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Refinement step | Cycle: final / Resolution: 2.8→29.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.801→2.873 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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