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- PDB-3k0a: Crystal structure of the phosphorylation-site mutant S431A of the... -
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Basic information
Entry | Database: PDB / ID: 3k0a | ||||||
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Title | Crystal structure of the phosphorylation-site mutant S431A of the KaiC circadian clock protein | ||||||
![]() | (Circadian clock protein kinase KaiC) x 2 | ||||||
![]() | CIRCADIAN CLOCK PROTEIN / TRANSFERASE / kaic / kinase / hexamer / ATP-binding / Biological rhythms / DNA-binding / Magnesium / Metal-binding / Nucleotide-binding / Phosphoprotein / Repressor / Serine/threonine-protein kinase / Transcription / Transcription regulation | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Pattanayek, R. / Egli, M. / Pattanayek, S. | ||||||
![]() | ![]() Title: Structures of KaiC Circadian Clock Mutant Proteins: A New Phosphorylation Site at T426 and Mechanisms of Kinase, ATPase and Phosphatase. Authors: Pattanayek, R. / Mori, T. / Xu, Y. / Pattanayek, S. / Johnson, C.H. / Egli, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 595.2 KB | Display | ![]() |
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PDB format | ![]() | 487.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 3.6 MB | Display | ![]() |
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Full document | ![]() | 3.8 MB | Display | |
Data in XML | ![]() | 98.2 KB | Display | |
Data in CIF | ![]() | 135.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3jzmC ![]() 3k09C ![]() 3k0cC ![]() 3k0eC ![]() 3k0fC ![]() 2gblS C: citing same article ( S: Starting model for refinement |
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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: 58216.734 Da / Num. of mol.: 1 / Mutation: S431A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: PCC7942 / Gene: kaic, see0011, Synpcc7942_1216 / Plasmid: PET3 / Production host: ![]() ![]() References: UniProt: Q79PF4, non-specific serine/threonine protein kinase | ||||||
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#2: Protein | Mass: 58136.750 Da / Num. of mol.: 5 / Mutation: S431A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: PCC7942 / Gene: kaic, see0011, Synpcc7942_1216 / Plasmid: PET3 / Production host: ![]() ![]() References: UniProt: Q79PF4, non-specific serine/threonine protein kinase #3: Chemical | ChemComp-ATP / #4: Chemical | ChemComp-MG / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.4 % |
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Crystal grow | Temperature: 291 K / pH: 4 Details: SODIUM FORMATE, GLYCEROL, pH 4, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 113.15 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR 300MM CCD / Detector: CCD / Date: Nov 7, 2007 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 62726 / % possible obs: 84.6 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 3.2→3.3 Å / Rmerge(I) obs: 0.085 / Mean I/σ(I) obs: 1 / % possible all: 37.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2GBL Resolution: 3→30 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 3→30 Å
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LS refinement shell | Resolution: 3→3.14 Å
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