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Open data
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Basic information
Entry | Database: PDB / ID: 2ju0 | ||||||
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Title | Structure of Yeast Frequenin bound to PdtIns 4-kinase | ||||||
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![]() | METAL BINDING PROTEIN/SIGNALING PROTEIN / EF-hand / calcium / PtdIns 4-kinase / frequenin / yeast / Lipoprotein / Membrane / Myristate / Nucleus / Phosphorylation / Transferase / METAL BINDING PROTEIN-SIGNALING PROTEIN COMPLEX | ||||||
Function / homology | ![]() cellular bud membrane / Inactivation, recovery and regulation of the phototransduction cascade / calcium sensitive guanylate cyclase activator activity / 1-phosphatidylinositol 4-kinase / 1-phosphatidylinositol 4-kinase activity / Synthesis of PIPs at the Golgi membrane / positive regulation of autophagosome assembly / phosphatidylinositol kinase activity / positive regulation of Golgi to plasma membrane protein transport / phosphatidylinositol-mediated signaling ...cellular bud membrane / Inactivation, recovery and regulation of the phototransduction cascade / calcium sensitive guanylate cyclase activator activity / 1-phosphatidylinositol 4-kinase / 1-phosphatidylinositol 4-kinase activity / Synthesis of PIPs at the Golgi membrane / positive regulation of autophagosome assembly / phosphatidylinositol kinase activity / positive regulation of Golgi to plasma membrane protein transport / phosphatidylinositol-mediated signaling / phosphatidylinositol phosphate biosynthetic process / regulation of signal transduction / enzyme activator activity / positive regulation of protein secretion / trans-Golgi network / endocytosis / Golgi membrane / intracellular membrane-bounded organelle / calcium ion binding / ATP binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Ames, J. | ||||||
![]() | ![]() Title: Structural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1). Authors: Strahl, T. / Huttner, I.G. / Lusin, J.D. / Osawa, M. / King, D. / Thorner, J. / Ames, J.B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 897.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 375.8 KB | Display | ![]() |
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Full document | ![]() | 692.1 KB | Display | |
Data in XML | ![]() | 95.7 KB | Display | |
Data in CIF | ![]() | 123.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 22036.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: FRQ1, NCS1 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Protein | Mass: 5631.423 Da / Num. of mol.: 1 / Fragment: Residues:121-174 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: PIK1 / Species (production host): Escherichia coli / Production host: ![]() ![]() References: UniProt: P39104, 1-phosphatidylinositol 4-kinase |
#3: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 15 / pH: 5.0 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software | Name: ![]() Developer: Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax Classification: processing |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 15 |