|Entry||Database: PDB / ID: 1fpu|
|Title||CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR|
|Components||PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL|
|Keywords||TRANSFERASE / kinase / kinase inhibitor / STI-571 / activation loop|
|Function / homology|
Function and homology information
delta-catenin binding / transitional one stage B cell differentiation / positive regulation of actin filament binding / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / B cell proliferation involved in immune response / positive regulation blood vessel branching / regulation of modification of synaptic structure ...delta-catenin binding / transitional one stage B cell differentiation / positive regulation of actin filament binding / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / B cell proliferation involved in immune response / positive regulation blood vessel branching / regulation of modification of synaptic structure / positive regulation of microtubule binding / positive regulation of Wnt signaling pathway, planar cell polarity pathway / microspike assembly / neuroepithelial cell differentiation / cerebellum morphogenesis / collateral sprouting / B-1 B cell homeostasis / actin filament branching / positive regulation of oxidoreductase activity / activated T cell proliferation / circulatory system development => GO:0072359 / neuropilin binding / neuropilin signaling pathway / bubble DNA binding / regulation of Cdc42 protein signal transduction / B cell proliferation / negative regulation of protein serine/threonine kinase activity / alpha-beta T cell differentiation / regulation of T cell differentiation / negative regulation of ubiquitin-protein transferase activity / regulation of microtubule polymerization / negative regulation of BMP signaling pathway / mitogen-activated protein kinase binding / proline-rich region binding / regulation of cellular senescence / syntaxin binding / DNA damage induced protein phosphorylation / positive regulation of osteoblast proliferation / negative regulation of cell-cell adhesion / platelet-derived growth factor receptor signaling pathway / negative regulation of cellular senescence / regulation of response to DNA damage stimulus / regulation of axon extension / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of cell migration involved in sprouting angiogenesis / phagocytosis / cell leading edge / negative regulation of long-term synaptic potentiation / positive regulation of interleukin-2 production / neuromuscular process controlling balance / Bergmann glial cell differentiation / positive regulation of focal adhesion assembly / positive regulation of actin cytoskeleton reorganization / negative regulation of endothelial cell apoptotic process / negative regulation of mitotic cell cycle / positive regulation of substrate adhesion-dependent cell spreading / endothelial cell migration / positive regulation of stress fiber assembly / four-way junction DNA binding / signal transduction in response to DNA damage / regulation of actin cytoskeleton organization / positive regulation of endothelial cell migration / substrate adhesion-dependent cell spreading / spleen development / negative regulation of I-kappaB kinase/NF-kappaB signaling / post-embryonic development / positive regulation of release of sequestered calcium ion into cytosol / positive regulation of mitotic cell cycle / SH2 domain binding / ruffle / negative regulation of ERK1 and ERK2 cascade / thymus development / phosphotyrosine residue binding / neuron differentiation / protein kinase C binding / ephrin receptor binding / neural tube closure / integrin-mediated signaling pathway / peptidyl-tyrosine autophosphorylation / positive regulation of interferon-gamma production / sequence-specific double-stranded DNA binding / actin cytoskeleton organization / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / regulation of cell cycle / establishment of protein localization / SH3 domain binding / autophagy / epidermal growth factor receptor signaling pathway / cellular response to hydrogen peroxide / positive regulation of neuron death / B cell receptor signaling pathway / growth cone / peptidyl-tyrosine phosphorylation / actin filament binding / endocytosis / actin cytoskeleton / positive regulation of cytosolic calcium ion concentration / positive regulation of peptidyl-tyrosine phosphorylation / regulation of cell population proliferation
SH2 domain / SH3-like domain superfamily / Protein kinase domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH3 domain / Tyrosine-protein kinase, active site / Protein kinase-like domain superfamily / F-actin binding / Protein kinase, ATP binding site / Tyrosine-protein kinase, catalytic domain ...SH2 domain / SH3-like domain superfamily / Protein kinase domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH3 domain / Tyrosine-protein kinase, active site / Protein kinase-like domain superfamily / F-actin binding / Protein kinase, ATP binding site / Tyrosine-protein kinase, catalytic domain / Tyrosine-protein kinase ABL1/transforming protein Abl / Tyrosine-protein kinase ABL, SH2 domain / SH2 domain superfamily / Protein tyrosine and serine/threonine kinase / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Tyrosine-protein kinase ABL1
|Biological species||Mus musculus (house mouse)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.4 Å|
|Authors||Schindler, T. / Bornmann, W. / Pellicena, P. / Miller, W.T. / Clarkson, B. / Kuriyan, J.|
|Citation||Journal: Science / Year: 2000|
Title: Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
Authors: Schindler, T. / Bornmann, W. / Pellicena, P. / Miller, W.T. / Clarkson, B. / Kuriyan, J.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
B: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
A: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
B: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
|Details||There are two kinase molecules in the asymmetric unit. The biological assembly is a monomer.|
Mass: 33743.523 Da / Num. of mol.: 2 / Fragment: KINASE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PFASTBAC / Cell line (production host): SF9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P00520, EC: 188.8.131.52
Mass: 382.418 Da / Num. of mol.: 2 / Fragment: 2-(PHENYLAMINO)-PYRIMIDINE COMPOUND / Source method: obtained synthetically / Formula: C22H18N6O
Details: chemically synthesized as described in Zimmermann J., Buchdunger E., Mett H., Meyer T., Lydon N.B. (1997) Bioorg. Med. Chem. Lett., Vol. 7, pp. 187
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.29 Å3/Da / Density % sol: 46.24 %|
|Crystal grow||Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.2 |
Details: PEG 4000, magnesium chloride, mes, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
*PLUSTemperature: 4 ℃ / pH: 8
|Components of the solutions|
|Diffraction||Mean temperature: 103 K|
|Diffraction source||Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9393|
|Detector||Type: BRANDEIS - B4 / Detector: CCD / Date: Sep 5, 1999|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.9393 Å / Relative weight: 1|
|Reflection||Resolution: 2.4→99 Å / Num. obs: 221636 / % possible obs: 98.7 % / Redundancy: 9.3 % / Biso Wilson estimate: 61 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 30.9|
|Reflection shell||Resolution: 2.4→2.49 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.216 / Num. unique all: 2190 / % possible all: 90.6|
*PLUSNum. obs: 24122 / Num. measured all: 221636
*PLUS% possible obs: 90.6 %
|Refinement||Resolution: 2.4→99 Å / Stereochemistry target values: Engh & Huber|
Details: Tight, noncrystallographic restraints were utilized throughout the refinement so that the final r.m.s. deviation between the two molecules is 0.05 and 0.04 Angstrom for the N-terminal and ...Details: Tight, noncrystallographic restraints were utilized throughout the refinement so that the final r.m.s. deviation between the two molecules is 0.05 and 0.04 Angstrom for the N-terminal and the C-terminal lobes, respectively (excluding residues 229 to 337, 252, 262, 271, 294, 306, 404, 447, 450, 466, and 491, which were built in different conformations in the two molecules). The electron density map was significantly weaker for one of the two molecules in the asymmetric unit (chain ID B), and all the analysis (cf. primary citation) relied on the better-ordered one (chain ID A).
|Refinement step||Cycle: LAST / Resolution: 2.4→99 Å|
|Refine LS restraints|
*PLUSName: CNS / Classification: refinement
*PLUSHighest resolution: 2.4 Å / Lowest resolution: 99 Å / Rfactor obs: 0.239
|Refine LS restraints|
*PLUSType: c_angle_deg / Dev ideal: 1.4
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