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- PDB-2g2h: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain -

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Basic information

Entry
Database: PDB / ID: 2g2h
TitleA Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
ComponentsAbl Tyrosine
KeywordsTRANSFERASE / 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 speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsLevinson, N.M. / Kuchment, O.
CitationJournal: 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.
Validation Report
SummaryFull reportAbout validation report
History
DepositionFeb 16, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 23, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Abl Tyrosine
B: Abl Tyrosine
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,2184
Polymers66,3642
Non-polymers8552
Water7,440413
1
A: Abl Tyrosine
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,6092
Polymers33,1821
Non-polymers4271
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Abl Tyrosine
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,6092
Polymers33,1821
Non-polymers4271
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)104.386, 131.487, 56.499
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/peptide Abl Tyrosine / p150 / c- ABL / Abelson murine leukemia viral oncogene homolog 1


Mass: 33181.957 Da / Num. of mol.: 2 / Fragment: Abl Tyrosine 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
#2: Chemical ChemComp-P16 / 6-(2,6-DICHLOROPHENYL)-2-{[3-(HYDROXYMETHYL)PHENYL]AMINO}-8-METHYLPYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE / PD166326


Mass: 427.283 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H16Cl2N4O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 413 / Source method: isolated from a natural source / Formula: H2O / Water

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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: 2.92 Å3/Da / Density % sol: 57.88 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 3.5
Details: 0.1M citric acid pH 3.5, 25% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 1.95→50 Å / Num. all: 57387 / Num. obs: 57387 / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.106 / Net I/σ(I): 11.04
Reflection shellResolution: 1.95→2.05 Å / Rmerge(I) obs: 0.414 / Mean I/σ(I) obs: 3.99 / % possible all: 99.8

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Processing

Software
NameVersionClassification
HKL-2000data collection
SCALEPACKdata scaling
PHASERphasing
CNS1.1refinement
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1M52
Resolution: 2→50 Å / Isotropic thermal model: isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.213 3664 random
Rwork0.193 --
All0.194 51722 -
Obs0.194 51722 -
Refinement stepCycle: LAST / Resolution: 2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4418 0 58 413 4889
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_angle_deg1.24

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