|Entry||Database: PDB / ID: 2g2f|
|Title||A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain|
|Keywords||TRANSFERASE / protein kinase|
|Function / homology|
Function and homology information
Role of ABL in ROBO-SLIT signaling / Regulation of actin dynamics for phagocytic cup formation / Myogenesis / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / RUNX2 regulates osteoblast differentiation / Cyclin D associated events in G1 / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / HDR through Single Strand Annealing (SSA) / RHO GTPases Activate WASPs and WAVEs ...Role of ABL in ROBO-SLIT signaling / Regulation of actin dynamics for phagocytic cup formation / Myogenesis / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / RUNX2 regulates osteoblast differentiation / Cyclin D associated events in G1 / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / HDR through Single Strand Annealing (SSA) / RHO GTPases Activate WASPs and WAVEs / mitochondrial depolarization / transitional one stage B cell differentiation / positive regulation of actin filament binding / DNA conformation change / activation of protein kinase C activity / negative regulation of phospholipase C activity / actin filament branching / positive regulation of interleukin-2 secretion / positive regulation blood vessel branching / nicotinate-nucleotide adenylyltransferase activity / B cell proliferation involved in immune response / positive regulation of microtubule binding / neuroepithelial cell differentiation / positive regulation of Wnt signaling pathway, planar cell polarity pathway / regulation of extracellular matrix organization / microspike assembly / regulation of modification of synaptic structure / cerebellum morphogenesis / collateral sprouting / B-1 B cell homeostasis / cardiovascular system development / alpha-beta T cell differentiation / positive regulation of oxidoreductase activity / activated T cell proliferation / bubble DNA binding / neuropilin signaling pathway / neuropilin binding / regulation of T cell differentiation / regulation of Cdc42 protein signal transduction / negative regulation of protein serine/threonine kinase activity / negative regulation of ubiquitin-protein transferase activity / regulation of microtubule polymerization / regulation of actin cytoskeleton reorganization / negative regulation of BMP signaling pathway / mitogen-activated protein kinase binding / sequence-specific double-stranded DNA binding / proline-rich region binding / positive regulation of interferon-gamma secretion / negative regulation of cell-cell adhesion / cellular response to dopamine / syntaxin binding / regulation of response to DNA damage stimulus / DNA damage induced protein phosphorylation / negative regulation of cellular senescence / positive regulation of osteoblast proliferation / cell leading edge / regulation of axon extension / actin monomer binding / positive regulation of cell migration involved in sprouting angiogenesis / platelet-derived growth factor receptor-beta signaling pathway / negative regulation of long-term synaptic potentiation / neuromuscular process controlling balance / Bergmann glial cell differentiation / mismatch repair / regulation of hematopoietic stem cell differentiation / positive regulation of focal adhesion assembly / positive regulation of muscle cell differentiation / positive regulation of actin cytoskeleton reorganization / regulation of endocytosis / regulation of cell adhesion / negative regulation of mitotic cell cycle / positive regulation of substrate adhesion-dependent cell spreading / regulation of cell motility / negative regulation of endothelial cell apoptotic process / four-way junction DNA binding / endothelial cell migration / positive regulation of stress fiber assembly / regulation of actin cytoskeleton organization / signal transduction in response to DNA damage / substrate adhesion-dependent cell spreading / regulation of autophagy / positive regulation of endothelial cell migration / cellular protein modification process / spleen development / SH2 domain binding / post-embryonic development / neural tube closure / positive regulation of mitotic cell cycle / negative regulation of I-kappaB kinase/NF-kappaB signaling / positive regulation of release of sequestered calcium ion into cytosol / thymus development / protein kinase C binding / negative regulation of ERK1 and ERK2 cascade / phosphotyrosine residue binding / ephrin receptor binding / integrin-mediated signaling pathway / actin cytoskeleton organization / autophagy / non-specific protein-tyrosine kinase / peptidyl-tyrosine autophosphorylation
Tyrosine-protein kinase ABL1/transforming protein Abl / Protein tyrosine kinase / Protein kinase, ATP binding site / Src homology 3 (SH3) domain profile. / Src homology 2 (SH2) domain profile. / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein kinases ATP-binding region signature. / F-actin binding / SH3 domain ...Tyrosine-protein kinase ABL1/transforming protein Abl / Protein tyrosine kinase / Protein kinase, ATP binding site / Src homology 3 (SH3) domain profile. / Src homology 2 (SH2) domain profile. / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein kinases ATP-binding region signature. / F-actin binding / SH3 domain / SH2 domain / SH2 domain superfamily / SH3-like domain superfamily / Tyrosine-protein kinase ABL, SH2 domain / Protein kinase-like domain superfamily / Tyrosine-protein kinase, catalytic domain / Protein kinase domain / Protein kinase domain profile. / Serine-threonine/tyrosine-protein kinase, catalytic domain / SH2 domain / SH3 domain / F-actin binding
Tyrosine-protein kinase ABL1
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å|
|Authors||Levinson, N.M. / Kuchment, O.|
|Citation||Journal: Plos Biol. / Year: 2006|
Title: A SRC-like inactive conformation in the abl tyrosine kinase domain.
Authors: Levinson, N.M. / Kuchment, O. / Shen, K. / Young, M.A. / Koldobskiy, M. / Karplus, M. / Cole, P.A. / Kuriyan, J.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Abl Kinase
B: Abl Kinase
C: ATP-Peptide Conjugate
A: Abl Kinase
C: ATP-Peptide Conjugate
B: Abl Kinase
Mass: 33181.957 Da / Num. of mol.: 2 / Fragment: Abl Kinase Domain / Mutation: H396P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ABL1, ABL, JTK7 / Production host: Escherichia coli (E. coli) / References: UniProt: P00519
Mass: 1194.420 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: solid phase peptide synthesis
|#3: Chemical|| ChemComp-AGS / ||#4: Chemical|| ChemComp-112 / ||#5: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.95 Å3/Da / Density % sol: 58.28 %|
|Crystal grow||Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.5 |
Details: 0.1M Bis-Tris pH 5.5, 25% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.115879 Å|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.115879 Å / Relative weight: 1|
|Reflection||Resolution: 2.7→50 Å / Num. all: 22582 / Num. obs: 22582 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.11 / Net I/σ(I): 10.7|
|Reflection shell||Resolution: 2.7→2.8 Å / Rmerge(I) obs: 0.494 / Mean I/σ(I) obs: 2.05 / % possible all: 98.2|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: PDB ENTRY 1M52
Resolution: 2.7→50 Å / Isotropic thermal model: isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
|Displacement parameters||Biso mean: 52.8 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.7→50 Å|
|Refine LS restraints|
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