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Yorodumi- PDB-2kit: The solution structure of the reduced yeast TOR1 FATC domain boun... -
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-Basic information
Entry | Database: PDB / ID: 2kit | ||||||
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Title | The solution structure of the reduced yeast TOR1 FATC domain bound to DPC micelles at 298K | ||||||
Components | Serine/threonine-protein kinase TOR1 | ||||||
Keywords | TRANSFERASE / protein / dpc micelle / membrane-mimetic / ATP-binding / Cell cycle / Cell membrane / Kinase / Membrane / Nucleotide-binding / Serine/threonine-protein kinase / Vacuole | ||||||
Function / homology | Function and homology information regulation of snRNA pseudouridine synthesis / regulation of sphingolipid biosynthetic process / mitochondria-nucleus signaling pathway / fungal-type cell wall organization / TORC2 complex / TORC1 complex / fungal-type vacuole membrane / negative regulation of macroautophagy / TOR signaling / nucleolar large rRNA transcription by RNA polymerase I ...regulation of snRNA pseudouridine synthesis / regulation of sphingolipid biosynthetic process / mitochondria-nucleus signaling pathway / fungal-type cell wall organization / TORC2 complex / TORC1 complex / fungal-type vacuole membrane / negative regulation of macroautophagy / TOR signaling / nucleolar large rRNA transcription by RNA polymerase I / translational initiation / response to endoplasmic reticulum stress / response to nutrient / negative regulation of autophagy / meiotic cell cycle / regulation of cell growth / ribosome biogenesis / cellular response to heat / cellular response to oxidative stress / peptidyl-serine phosphorylation / endosome membrane / regulation of cell cycle / non-specific serine/threonine protein kinase / protein kinase activity / Golgi membrane / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / DNA damage response / protein-containing complex binding / ATP binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Dames, S.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Structural Basis for the Association of the Redox-sensitive Target of Rapamycin FATC Domain with Membrane-mimetic Micelles. Authors: Dames, S.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kit.cif.gz | 213.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kit.ent.gz | 183.2 KB | Display | PDB format |
PDBx/mmJSON format | 2kit.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ki/2kit ftp://data.pdbj.org/pub/pdb/validation_reports/ki/2kit | HTTPS FTP |
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-Related structure data
Related structure data | 2kioC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3963.473 Da / Num. of mol.: 1 / Fragment: yeast TOR1 FATC domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: DRR1, J1803, TOR1, YJR066W / Plasmid: pGEV2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): Rosetta (DE3) References: UniProt: P35169, non-specific serine/threonine protein kinase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: The solution struture of the reduced yeast TOR1 FATC domain bound to DPC micelles at 298K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM [U-13C; U-15N] y1fatc-1, 95% H2O/5% D2O / Solvent system: 95% H2O/5% D2O |
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Sample | Conc.: 0.5 mM / Component: y1fatc-1 / Isotopic labeling: [U-13C; U-15N] |
Sample conditions | Ionic strength: 150 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1167 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Maximum upper distance constraint violation: 0.5 Å |