[English] 日本語
![](img/lk-miru.gif)
- PDB-2qlv: Crystal structure of the heterotrimer core of the S. cerevisiae A... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2qlv | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the heterotrimer core of the S. cerevisiae AMPK homolog SNF1 | ||||||
![]() |
| ||||||
![]() | Transferase/Protein binding / heterotrimer / ATP-binding / Carbohydrate metabolism / Kinase / Membrane / Nucleotide-binding / Nucleus / Phosphorylation / Serine/threonine-protein kinase / Transferase / Lipoprotein / Myristate / CBS domain / Transcription / Transcription regulation / Transferase-Protein binding COMPLEX | ||||||
Function / homology | ![]() fungal-type cell wall assembly / positive regulation of pseudohyphal growth / positive regulation of filamentous growth of a population of unicellular organisms in response to starvation / AMPK inhibits chREBP transcriptional activation activity / Energy dependent regulation of mTOR by LKB1-AMPK / single-species surface biofilm formation / regulation of cellular response to glucose starvation / regulation of invasive growth in response to glucose limitation / cellular bud neck septin ring / Carnitine metabolism ...fungal-type cell wall assembly / positive regulation of pseudohyphal growth / positive regulation of filamentous growth of a population of unicellular organisms in response to starvation / AMPK inhibits chREBP transcriptional activation activity / Energy dependent regulation of mTOR by LKB1-AMPK / single-species surface biofilm formation / regulation of cellular response to glucose starvation / regulation of invasive growth in response to glucose limitation / cellular bud neck septin ring / Carnitine metabolism / invasive growth in response to glucose limitation / Macroautophagy / peroxisome organization / filamentous growth / nucleotide-activated protein kinase complex / protein kinase regulator activity / enzyme-substrate adaptor activity / vacuolar membrane / AMP-activated protein kinase activity / nuclear envelope lumen / AMP binding / establishment of mitotic spindle orientation / positive regulation of macroautophagy / response to unfolded protein / regulation of protein-containing complex assembly / cellular response to glucose starvation / positive regulation of gluconeogenesis / response to endoplasmic reticulum stress / protein serine/threonine kinase activator activity / guanyl-nucleotide exchange factor activity / molecular function activator activity / autophagy / nuclear membrane / negative regulation of translation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / regulation of transcription by RNA polymerase II / protein kinase binding / signal transduction / mitochondrion / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Amodeo, G.A. / Rudolph, M.J. / Tong, L. | ||||||
![]() | ![]() Title: Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1. Authors: Amodeo, G.A. / Rudolph, M.J. / Tong, L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 248.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 197.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 468.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 528.9 KB | Display | |
Data in XML | ![]() | 49.5 KB | Display | |
Data in CIF | ![]() | 67.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is that of a trimer consisting of Snf1, Sip2, and Snf4. |
-
Components
#1: Protein | Mass: 19596.268 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF1, CAT1, CCR1, GLC2, PAS14 / Plasmid: pET 28a / Production host: ![]() ![]() References: UniProt: P06782, non-specific serine/threonine protein kinase #2: Protein | Mass: 28956.588 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SIP2, SPM2 / Plasmid: pET 28a / Production host: ![]() ![]() #3: Protein | Mass: 35625.066 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF4, CAT3 / Plasmid: pET 28a / Production host: ![]() ![]() #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.24 % |
---|---|
Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 250 mM ammonium citrate, 15% PEG3350, 1mM AMP, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 21, 2007 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Cryogenically cooled double crystal monochrometer with horizontal focusing sagittal bend second mono crystal with 4:1 magnification ratio and vertically focusing mirror Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.0809 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Redundancy: 2.9 % / Av σ(I) over netI: 17.4 / Number: 130084 / Rmerge(I) obs: 0.071 / Χ2: 1.02 / D res high: 2.6 Å / D res low: 30 Å / Num. obs: 44415 / % possible obs: 93.3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.6→30 Å / Num. obs: 44415 / % possible obs: 93.3 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.071 / Χ2: 1.018 / Net I/σ(I): 17.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.385 / Num. unique all: 3361 / Χ2: 1.075 / % possible all: 71.3 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| ||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 45.919 Å2 / ksol: 0.311 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 66.3 Å2
| ||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→29.54 Å
| ||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.6→2.69 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 10
| ||||||||||||||||||||||||||||||||||||
Xplor file |
|