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- PDB-4xey: Crystal structure of an SH2-kinase domain construct of c-Abl tyro... -

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Basic information

Entry
Database: PDB / ID: 4xey
TitleCrystal structure of an SH2-kinase domain construct of c-Abl tyrosine kinase
ComponentsTyrosine-protein kinase ABL1
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / tyrosine kinase / kinase domain / SH2 domain / dasatinib / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


positive regulation of actin filament binding / positive regulation of oxidoreductase activity / protein localization to cytoplasmic microtubule plus-end / negative regulation of ubiquitin-protein transferase activity / DN4 thymocyte differentiation / response to epinephrine / activation of protein kinase C activity / phospholipase C-inhibiting G protein-coupled receptor signaling pathway / podocyte apoptotic process / transitional one stage B cell differentiation ...positive regulation of actin filament binding / positive regulation of oxidoreductase activity / protein localization to cytoplasmic microtubule plus-end / negative regulation of ubiquitin-protein transferase activity / DN4 thymocyte differentiation / response to epinephrine / activation of protein kinase C activity / phospholipase C-inhibiting G protein-coupled receptor signaling pathway / podocyte apoptotic process / transitional one stage B cell differentiation / delta-catenin binding / Role of ABL in ROBO-SLIT signaling / regulation of postsynaptic specialization assembly / regulation of modification of synaptic structure / nicotinate-nucleotide adenylyltransferase activity / DNA conformation change / positive regulation of microtubule binding / neuroepithelial cell differentiation / B cell proliferation involved in immune response / positive regulation of Wnt signaling pathway, planar cell polarity pathway / cerebellum morphogenesis / positive regulation of extracellular matrix organization / microspike assembly / positive regulation of blood vessel branching / B-1 B cell homeostasis / neuropilin signaling pathway / neuropilin binding / bubble DNA binding / mitochondrial depolarization / negative regulation of protein serine/threonine kinase activity / activated T cell proliferation / positive regulation of establishment of T cell polarity / cellular response to dopamine / regulation of cell motility / proline-rich region binding / regulation of Cdc42 protein signal transduction / syntaxin binding / mitogen-activated protein kinase binding / regulation of hematopoietic stem cell differentiation / myoblast proliferation / alpha-beta T cell differentiation / positive regulation of dendrite development / regulation of T cell differentiation / regulation of axon extension / cardiac muscle cell proliferation / HDR through Single Strand Annealing (SSA) / positive regulation of cell migration involved in sprouting angiogenesis / negative regulation of cell-cell adhesion / Myogenesis / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of osteoblast proliferation / RUNX2 regulates osteoblast differentiation / regulation of microtubule polymerization / Fc-gamma receptor signaling pathway involved in phagocytosis / associative learning / Bergmann glial cell differentiation / regulation of endocytosis / neuromuscular process controlling balance / negative regulation of mitotic cell cycle / negative regulation of long-term synaptic potentiation / negative regulation of cellular senescence / actin monomer binding / negative regulation of BMP signaling pathway / endothelial cell migration / positive regulation of focal adhesion assembly / signal transduction in response to DNA damage / canonical NF-kappaB signal transduction / RHO GTPases Activate WASPs and WAVEs / positive regulation of T cell migration / BMP signaling pathway / regulation of cell adhesion / negative regulation of double-strand break repair via homologous recombination / mismatch repair / negative regulation of endothelial cell apoptotic process / peptidyl-tyrosine autophosphorylation / four-way junction DNA binding / spleen development / cellular response to transforming growth factor beta stimulus / positive regulation of stress fiber assembly / positive regulation of vasoconstriction / ruffle / ephrin receptor binding / positive regulation of substrate adhesion-dependent cell spreading / phosphotyrosine residue binding / actin filament polymerization / positive regulation of endothelial cell migration / ERK1 and ERK2 cascade / positive regulation of interleukin-2 production / response to endoplasmic reticulum stress / positive regulation of mitotic cell cycle / substrate adhesion-dependent cell spreading / SH2 domain binding / post-embryonic development / positive regulation of release of sequestered calcium ion into cytosol / thymus development / protein kinase C binding / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / regulation of autophagy / integrin-mediated signaling pathway / establishment of localization in cell
Similarity search - Function
F-actin binding / F-actin binding / F-actin binding domain (FABD) / Tyrosine-protein kinase ABL, SH2 domain / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...F-actin binding / F-actin binding / F-actin binding domain (FABD) / Tyrosine-protein kinase ABL, SH2 domain / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-1N1 / Tyrosine-protein kinase ABL1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.891 Å
AuthorsLorenz, S. / Deng, P. / Kuriyan, J.
Funding support United States, 1items
OrganizationGrant numberCountry
Leukemia & Lymphoma Society7393-06 United States
CitationJournal: Biochem.J. / Year: 2015
Title: Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity.
Authors: Lorenz, S. / Deng, P. / Hantschel, O. / Superti-Furga, G. / Kuriyan, J.
History
DepositionDec 25, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 1, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 3, 2015Group: Database references
Revision 1.2Sep 27, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Sep 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: Tyrosine-protein kinase ABL1
A: Tyrosine-protein kinase ABL1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,6964
Polymers93,7202
Non-polymers9762
Water00
1
A: Tyrosine-protein kinase ABL1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,3482
Polymers46,8601
Non-polymers4881
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Tyrosine-protein kinase ABL1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,3482
Polymers46,8601
Non-polymers4881
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)114.118, 125.449, 56.232
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein Tyrosine-protein kinase ABL1 / Abelson murine leukemia viral oncogene homolog 1 / Abelson tyrosine-protein kinase 1 / Proto- ...Abelson murine leukemia viral oncogene homolog 1 / Abelson tyrosine-protein kinase 1 / Proto-oncogene c-Abl / p150


Mass: 46860.000 Da / Num. of mol.: 2 / Fragment: UNP residues 119-515
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ABL1, ABL, JTK7 / Plasmid: pET21d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P00519, non-specific protein-tyrosine kinase
#2: Chemical ChemComp-1N1 / N-(2-CHLORO-6-METHYLPHENYL)-2-({6-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]-2-METHYLPYRIMIDIN-4-YL}AMINO)-1,3-THIAZOLE-5-CARBOXAMIDE / Dasatinib


Mass: 488.006 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H26ClN7O2S / Comment: medication*YM

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.15 Å3/Da / Density % sol: 42.72 % / Description: needle
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 0.1M sodium citrate, 8% PEG 8000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.1159 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 10, 2009
RadiationMonochromator: double flat crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1159 Å / Relative weight: 1
ReflectionResolution: 2.89→46.96 Å / Num. obs: 18720 / % possible obs: 99.6 % / Redundancy: 4 % / Rsym value: 0.145 / Net I/σ(I): 9.24
Reflection shellResolution: 2.89→2.95 Å / Redundancy: 4 % / Mean I/σ(I) obs: 2.1 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
HKL-20002.3.6data reduction
HKL-20002.3.6data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2GQG,1OPK

2gqg

1opk


Resolution: 2.891→46.799 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2593 957 5.13 %
Rwork0.2308 --
obs0.2323 18647 99.54 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.891→46.799 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5114 0 66 0 5180
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035315
X-RAY DIFFRACTIONf_angle_d0.8057195
X-RAY DIFFRACTIONf_dihedral_angle_d14.1961971
X-RAY DIFFRACTIONf_chiral_restr0.029762
X-RAY DIFFRACTIONf_plane_restr0.003902
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.891-3.04340.30841430.30012406X-RAY DIFFRACTION97
3.0434-3.2340.3131510.28582479X-RAY DIFFRACTION100
3.234-3.48370.29361270.25152503X-RAY DIFFRACTION100
3.4837-3.83410.28581350.22782514X-RAY DIFFRACTION100
3.8341-4.38850.23421280.21582534X-RAY DIFFRACTION100
4.3885-5.52770.23671260.20762577X-RAY DIFFRACTION100
5.5277-46.80550.22571470.21452677X-RAY DIFFRACTION100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.03450.0747-0.02750.26150.0740.10910.16740.12110.2261-0.6558-0.2848-0.79770.11570.9471-00.81390.15050.15641.18810.02731.0322-18.2156-14.2157-17.3085
21.9949-0.4505-0.18282.55170.3731.9904-0.0298-0.0940.29520.0351-0.0321-0.1675-0.33370.149700.25670.0393-0.00730.2730.01150.3-16.8443-43.046512.8914
30.82930.1007-0.14521.6338-0.22552.5763-0.00470.0373-0.0651-0.04760.0127-0.11520.24870.207100.18470.053-0.00120.1791-0.03090.1969-45.9946-19.566813.169
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'B' and resid 141 through 238)
2X-RAY DIFFRACTION2(chain 'A' and resid 250 through 522)
3X-RAY DIFFRACTION3(chain 'B' and resid 251 through 523)

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