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- PDB-5x02: Crystal structure of the FLT3 kinase domain bound to the inhibito... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5x02 | ||||||
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Title | Crystal structure of the FLT3 kinase domain bound to the inhibitor FF-10101 | ||||||
![]() | Receptor-type tyrosine-protein kinase FLT3 | ||||||
![]() | TRANSFERASE/TRANSFERASE INIHIBITOR / tyrosine kinase / transferase / irreversible inhibitor complex / kinase catalytic domain / TRANSFERASE-TRANSFERASE INIHIBITOR complex | ||||||
Function / homology | ![]() FLT3 mutants bind TKIs / KW2449-resistant FLT3 mutants / semaxanib-resistant FLT3 mutants / crenolanib-resistant FLT3 mutants / gilteritinib-resistant FLT3 mutants / lestaurtinib-resistant FLT3 mutants / midostaurin-resistant FLT3 mutants / pexidartinib-resistant FLT3 mutants / ponatinib-resistant FLT3 mutants / quizartinib-resistant FLT3 mutants ...FLT3 mutants bind TKIs / KW2449-resistant FLT3 mutants / semaxanib-resistant FLT3 mutants / crenolanib-resistant FLT3 mutants / gilteritinib-resistant FLT3 mutants / lestaurtinib-resistant FLT3 mutants / midostaurin-resistant FLT3 mutants / pexidartinib-resistant FLT3 mutants / ponatinib-resistant FLT3 mutants / quizartinib-resistant FLT3 mutants / sorafenib-resistant FLT3 mutants / sunitinib-resistant FLT3 mutants / tandutinib-resistant FLT3 mutants / linifanib-resistant FLT3 mutants / tamatinib-resistant FLT3 mutants / leukocyte homeostasis / lymphocyte proliferation / pro-B cell differentiation / common myeloid progenitor cell proliferation / dendritic cell differentiation / vascular endothelial growth factor receptor activity / phosphatidylinositol 3-kinase activator activity / STAT5 Activation / nuclear glucocorticoid receptor binding / myeloid progenitor cell differentiation / FLT3 signaling through SRC family kinases / cellular response to glucocorticoid stimulus / cytokine receptor activity / STAT5 activation downstream of FLT3 ITD mutants / growth factor binding / cellular response to cytokine stimulus / hemopoiesis / PI3K Cascade / animal organ regeneration / Signaling by FLT3 ITD and TKD mutants / positive regulation of tyrosine phosphorylation of STAT protein / FLT3 signaling by CBL mutants / cell surface receptor protein tyrosine kinase signaling pathway / : / Negative regulation of FLT3 / FLT3 Signaling / transmembrane receptor protein tyrosine kinase activity / B cell differentiation / positive regulation of MAP kinase activity / receptor protein-tyrosine kinase / cytokine-mediated signaling pathway / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / : / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / regulation of apoptotic process / protein tyrosine kinase activity / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / endosome membrane / endoplasmic reticulum lumen / positive regulation of cell population proliferation / protein-containing complex binding / endoplasmic reticulum / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fujikawa, N. / Hirano, D. / Takasaki, M. / Terada, D. / Hagiwara, S. / Park, S.-Y. / Sugiyama, K. | ||||||
![]() | ![]() Title: A novel irreversible FLT3 inhibitor, FF-10101, shows excellent efficacy against AML cells withFLT3mutations. Authors: Yamaura, T. / Nakatani, T. / Uda, K. / Ogura, H. / Shin, W. / Kurokawa, N. / Saito, K. / Fujikawa, N. / Date, T. / Takasaki, M. / Terada, D. / Hirai, A. / Akashi, A. / Chen, F. / Adachi, Y. ...Authors: Yamaura, T. / Nakatani, T. / Uda, K. / Ogura, H. / Shin, W. / Kurokawa, N. / Saito, K. / Fujikawa, N. / Date, T. / Takasaki, M. / Terada, D. / Hirai, A. / Akashi, A. / Chen, F. / Adachi, Y. / Ishikawa, Y. / Hayakawa, F. / Hagiwara, S. / Naoe, T. / Kiyoi, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.7 KB | Display | ![]() |
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PDB format | ![]() | 55.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 662.5 KB | Display | ![]() |
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Full document | ![]() | 665.7 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 17.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1rjbS 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: 40010.543 Da / Num. of mol.: 1 / Fragment: UNP residues 564-710,762-958 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P36888, receptor protein-tyrosine kinase | ||
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#2: Chemical | ChemComp-F6M / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.02 Å3/Da / Density % sol: 59.21 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7 Details: 2.2-2.4M Na/K Phosphate, 0.1M CAPS (pH6.7), 0.2M Litium Sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 19, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 19769 / % possible obs: 99.5 % / Redundancy: 14.2 % / Net I/σ(I): 57.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1RJB Resolution: 2.401→36.906 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 28.96
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso max: 141.59 Å2 / Biso mean: 74.3646 Å2 / Biso min: 42.61 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.401→36.906 Å
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