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- PDB-1e8z: Structure determinants of phosphoinositide 3-kinase inhibition by... -
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Basic information
Entry | Database: PDB / ID: 1e8z | ||||||
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Title | Structure determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin and staurosporine | ||||||
![]() | PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT | ||||||
![]() | TRANSFERASE / PHOSPHOINOSITIDE 3-KINASE GAMMA / SECONDARY MESSENGER GENERATION / PI3K / PI 3K / STAUROSPORINE | ||||||
Function / homology | ![]() secretory granule localization / negative regulation of triglyceride catabolic process / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis ...secretory granule localization / negative regulation of triglyceride catabolic process / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis / negative regulation of fibroblast apoptotic process / phosphatidylinositol 3-kinase complex, class IB / sphingosine-1-phosphate receptor signaling pathway / phosphatidylinositol 3-kinase complex, class IA / dendritic cell chemotaxis / 1-phosphatidylinositol-4-phosphate 3-kinase activity / 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity / phosphatidylinositol-4,5-bisphosphate 3-kinase / phosphatidylinositol 3-kinase / phosphatidylinositol-3-phosphate biosynthetic process / 1-phosphatidylinositol-3-kinase activity / mast cell degranulation / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / hepatocyte apoptotic process / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / Synthesis of PIPs at the plasma membrane / phosphatidylinositol-mediated signaling / phosphatidylinositol phosphate biosynthetic process / regulation of angiogenesis / T cell proliferation / cellular response to cAMP / GPVI-mediated activation cascade / T cell activation / ephrin receptor binding / positive regulation of endothelial cell migration / phosphatidylinositol 3-kinase/protein kinase B signal transduction / neutrophil chemotaxis / positive regulation of cytokine production / positive regulation of MAP kinase activity / platelet aggregation / endocytosis / G beta:gamma signalling through PI3Kgamma / Signaling by CSF1 (M-CSF) in myeloid cells / kinase activity / positive regulation of cytosolic calcium ion concentration / angiogenesis / adaptive immune response / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / non-specific serine/threonine protein kinase / protein kinase activity / inflammatory response / immune response / G protein-coupled receptor signaling pathway / phosphorylation / innate immune response / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / identical protein binding / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Walker, E.H. / Pacold, M.E. / Perisic, O. / Stephens, L. / Hawkins, P.T. / Wymann, M.P. / Williams, R.L. | ||||||
![]() | ![]() Title: Structural Determinations of Phosphoinositide 3-Kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine Authors: Walker, E.H. / Pacold, M.E. / Perisic, O. / Stephens, L. / Hawkins, P.T. / Whymann, M.P. / Williams, R.L. #1: Journal: Nature / Year: 1999 Title: Structural Insights Into Phosphoinositide 3-Kinase Catalysis and Signalling Authors: Walker, E.H. / Perisic, O. / Ried, C. / Stephens, L. / Williams, R.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 186 KB | Display | ![]() |
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PDB format | ![]() | 143.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 859.3 KB | Display | ![]() |
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Full document | ![]() | 899 KB | Display | |
Data in XML | ![]() | 34.6 KB | Display | |
Data in CIF | ![]() | 46.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1e7uC ![]() 1e7vC ![]() 1e8wC ![]() 1e8xC ![]() 1e8yC ![]() 1e90C ![]() 1qmm 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: 110756.164 Da / Num. of mol.: 1 / Fragment: PI3-KINASE P110 SUBUNIT GAMMA / Mutation: YES Source method: isolated from a genetically manipulated source Details: STAUROSPORINE / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-STU / |
#3: Water | ChemComp-HOH / |
Sequence details | THE NATIVE PROTEIN WAS MUTATED BY DELETION OF RESIDUES 1-143. A C-TERMINAL 6-HIS TAG WAS ATTACHED ...THE NATIVE PROTEIN WAS MUTATED BY DELETION OF RESIDUES 1-143. A C-TERMINAL 6-HIS TAG WAS ATTACHED AS WAS A N-TERMINAL METHIONINE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.788 Å3/Da / Density % sol: 55.92 % | ||||||||||||||||||||
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Crystal grow | pH: 7.25 / Details: 19% PEG 4000, 0.25 M (NH4)2SO4, 0.1 M TRIS PH 7.2 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / pH: 7.2 / Method: vapor diffusion, hanging drop / Details: used hair seeding | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 15, 1999 / Details: BENT MIRROR |
Radiation | Monochromator: DIAMOND C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→26.68 Å / Num. obs: 32910 / % possible obs: 87.7 % / Observed criterion σ(I): 0 / Redundancy: 3.14 % / Biso Wilson estimate: 36.9 Å2 / Rmerge(I) obs: 0.087 / Net I/σ(I): 18.94 |
Reflection shell | Resolution: 2.4→2.52 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 3.78 / Rsym value: 0.219 / % possible all: 57.7 |
Reflection | *PLUS Num. measured all: 103376 |
Reflection shell | *PLUS % possible obs: 57.7 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QMM ![]() 1qmm Resolution: 2.4→60.84 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 2381808.88 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 49.4885 Å2 / ksol: 0.3595 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→60.84 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.55 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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