|Entry||Database: PDB / ID: 2fo0|
|Title||Organization of the SH3-SH2 Unit in Active and Inactive Forms of the c-Abl Tyrosine Kinase|
|Components||Proto-oncogene tyrosine-protein kinase ABL1 (1B ISOFORM)|
|Keywords||TRANSFERASE / N-terminal cap / autoinhibition / myristoylation / SH3-SH2 clamp / phosphoserine|
|Function / homology|
Function and homology information
mitochondrial depolarization / positive regulation of interleukin-2 production => GO:0032743 / positive regulation of actin filament binding / transitional one stage B cell differentiation / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / positive regulation blood vessel branching ...mitochondrial depolarization / positive regulation of interleukin-2 production => GO:0032743 / positive regulation of actin filament binding / transitional one stage B cell differentiation / DNA conformation change / negative regulation of phospholipase C activity / regulation of extracellular matrix organization / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / positive regulation blood vessel branching / B cell proliferation involved in immune response / 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 / 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 / regulation of actin cytoskeleton reorganization / positive regulation of interferon-gamma production => GO:0032729 / mitogen-activated protein kinase binding / proline-rich region binding / syntaxin binding / DNA damage induced protein phosphorylation / cellular response to dopamine / positive regulation of osteoblast proliferation / negative regulation of cell-cell adhesion / 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 / cell leading edge / negative regulation of long-term synaptic potentiation / actin monomer binding / neuromuscular process controlling balance / Bergmann glial cell differentiation / positive regulation of focal adhesion assembly / regulation of endocytosis / positive regulation of actin cytoskeleton reorganization / mismatch repair / regulation of cell adhesion / regulation of hematopoietic stem cell differentiation / negative regulation of endothelial cell apoptotic process / regulation of cell motility / negative regulation of mitotic cell cycle / positive regulation of substrate adhesion-dependent cell spreading / endothelial cell migration / positive regulation of muscle cell differentiation / 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 / regulation of autophagy / cellular protein modification process / 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 / negative regulation of ERK1 and ERK2 cascade / thymus development / phosphotyrosine residue binding / protein kinase C binding / neural tube closure / ephrin receptor binding / integrin-mediated signaling pathway / peptidyl-tyrosine autophosphorylation / sequence-specific double-stranded DNA binding / actin cytoskeleton organization / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / establishment of protein localization / SH3 domain binding / postsynapse / autophagy / cell cycle arrest / epidermal growth factor receptor signaling pathway / cellular response to hydrogen peroxide / positive regulation of neuron death / B cell receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis
Tyrosine-protein kinase, catalytic domain / SH2 domain / Protein kinase domain / SH2 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 / Protein kinase domain / SH2 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 ABL1/transforming protein Abl / Tyrosine-protein kinase ABL, SH2 domain / Protein tyrosine and serine/threonine kinase / SH3-like domain superfamily / SH2 domain superfamily / SH3 domain / SH2 domain / SHC Adaptor Protein / SH3 Domains / SH3 type barrels. / Roll / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Tyrosine-protein kinase ABL1 / Tyrosine-protein kinase ABL1
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.27 Å|
|Authors||Nagar, B. / Hantschel, O. / Seeliger, M. / Davies, J.M. / Weis, W.I. / Superti-Furga, G. / Kuriyan, J.|
|Citation||Journal: Mol.Cell / Year: 2006|
Title: Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase.
Authors: Nagar, B. / Hantschel, O. / Seeliger, M. / Davies, J.M. / Weis, W.I. / Superti-Furga, G. / Kuriyan, J.
SummaryFull reportAbout validation report
|Remark 999||SEQUENCE Residues 15-56 of the original protein sequence were deleted. Myristoyl group (MYR) is ...SEQUENCE Residues 15-56 of the original protein sequence were deleted. Myristoyl group (MYR) is covalently attached to the N-terminus of the protein.|
|Structure viewer||Molecule: |
Downloads & links
A: Proto-oncogene tyrosine-protein kinase ABL1 (1B ISOFORM)
|#1: Protein|| |
Mass: 56452.371 Da / Num. of mol.: 1
Fragment: Abl N-cap (residues 1-531, residues 15-56 deleted)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: c-Abl / Plasmid: PFASTBAC1 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P00519-2, UniProt: P00519*PLUS, EC: 126.96.36.199
|#2: Chemical|| ChemComp-MYR / |
|#3: Chemical|| ChemComp-P16 / |
|#4: Chemical||#5: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.5 Å3/Da / Density % sol: 50.78 %|
|Crystal grow||Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: 20% PEG 10000, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1.1 Å|
|Detector||Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 24, 2003|
|Radiation||Monochromator: Double crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.1 Å / Relative weight: 1|
|Reflection||Resolution: 2.27→48.14 Å / Num. all: 25639 / Num. obs: 25639 / % possible obs: 94.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.1 % / Biso Wilson estimate: 17.2 Å2 / Rsym value: 0.095 / Net I/σ(I): 14.6|
|Reflection shell||Resolution: 2.27→2.35 Å / Redundancy: 2.5 % / Mean I/σ(I) obs: 3.2 / Num. unique all: 2026 / Rsym value: 0.289 / % possible all: 76.5|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: PDB ENTRY 1OPK
Resolution: 2.27→48.14 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 318702.33 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 33.6955 Å2 / ksol: 0.376791 e/Å3|
|Displacement parameters||Biso mean: 38.8 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.27→48.14 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 2.27→2.41 Å / Rfactor Rfree error: 0.018 / Total num. of bins used: 6 |
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