+Open data
-Basic information
Entry | Database: PDB / ID: 2og8 | ||||||
---|---|---|---|---|---|---|---|
Title | crystal structure of aminoquinazoline 36 bound to Lck | ||||||
Components | Proto-oncogene tyrosine-protein kinase LCK | ||||||
Keywords | TRANSFERASE / Lck / Kinase domain | ||||||
Function / homology | Function and homology information regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / Fc-gamma receptor signaling pathway / CD28 co-stimulation / FLT3 signaling through SRC family kinases / intracellular zinc ion homeostasis / CD4 receptor binding / Nef and signal transduction / Nef Mediated CD4 Down-regulation / Interleukin-2 signaling ...regulation of lymphocyte activation / positive regulation of leukocyte cell-cell adhesion / Fc-gamma receptor signaling pathway / CD28 co-stimulation / FLT3 signaling through SRC family kinases / intracellular zinc ion homeostasis / CD4 receptor binding / Nef and signal transduction / Nef Mediated CD4 Down-regulation / Interleukin-2 signaling / CD28 dependent Vav1 pathway / positive regulation of heterotypic cell-cell adhesion / protein serine/threonine phosphatase activity / Regulation of KIT signaling / CTLA4 inhibitory signaling / phospholipase activator activity / positive regulation of T cell receptor signaling pathway / leukocyte migration / pericentriolar material / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / phospholipase binding / PECAM1 interactions / CD28 dependent PI3K/Akt signaling / RHOH GTPase cycle / hemopoiesis / Generation of second messenger molecules / immunological synapse / T cell differentiation / PD-1 signaling / CD8 receptor binding / phosphatidylinositol 3-kinase binding / positive regulation of intrinsic apoptotic signaling pathway / peptidyl-tyrosine autophosphorylation / release of sequestered calcium ion into cytosol / GPVI-mediated activation cascade / T cell costimulation / extrinsic component of cytoplasmic side of plasma membrane / SH2 domain binding / phosphotyrosine residue binding / T cell receptor binding / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / B cell receptor signaling pathway / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / Signaling by SCF-KIT / platelet activation / peptidyl-tyrosine phosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / activation of cysteine-type endopeptidase activity involved in apoptotic process / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of T cell activation / Downstream TCR signaling / PIP3 activates AKT signaling / DAP12 signaling / ATPase binding / T cell receptor signaling pathway / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein phosphatase binding / protein tyrosine kinase activity / intracellular signal transduction / response to xenobiotic stimulus / membrane raft / signaling receptor binding / protein phosphorylation / innate immune response / protein kinase binding / extracellular exosome / ATP binding / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Huang, X. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2006 Title: Discovery of Aminoquinazolines as Potent, Orally Bioavailable Inhibitors of Lck: Synthesis, SAR, and in Vivo Anti-Inflammatory Activity Authors: DiMauro, E.F. / Newcomb, J. / Nunes, J.J. / Bemis, J.E. / Boucher, C. / Buchanan, J.L. / Buckner, W.H. / Cee, V.J. / Chai, L. / Deak, H.L. / Epstein, L.F. / Faust, T. / Gallant, P. / Geuns- ...Authors: DiMauro, E.F. / Newcomb, J. / Nunes, J.J. / Bemis, J.E. / Boucher, C. / Buchanan, J.L. / Buckner, W.H. / Cee, V.J. / Chai, L. / Deak, H.L. / Epstein, L.F. / Faust, T. / Gallant, P. / Geuns-Meyer, S.D. / Gore, A. / Gu, Y. / Henkle, B. / Hodous, B.L. / Hsieh, F. / Huang, X. / Kim, J.L. / Lee, J.H. / Martin, M.W. / Masse, C.E. / McGowan, D.C. / Metz, D. / Morgenstern, K.A. / Oliveira-dos-Santos, A. / Patel, V.F. / Powers, D. / Rose, P.E. / Schneider, S. / Tomlinson, S.A. / Tudor, Y.Y. / Turci, S.M. / Welcher, A.A. / White, R.D. / Zhao, H. / Zhu, L. / Zhu, X. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2og8.cif.gz | 116.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2og8.ent.gz | 89.9 KB | Display | PDB format |
PDBx/mmJSON format | 2og8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/og/2og8 ftp://data.pdbj.org/pub/pdb/validation_reports/og/2og8 | HTTPS FTP |
---|
-Related structure data
Related structure data | 2ofvC 1qpcS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
| ||||||||
Details | The Biological Assembly is a monomer. |
-Components
#1: Protein | Mass: 30516.955 Da / Num. of mol.: 2 / Fragment: Lck kinase domain, residues 236-498 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LCK / Production host: Insect Cell References: UniProt: P06239, non-specific protein-tyrosine kinase #2: Chemical | #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.81 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 1.0 M LiCl, 10-22.5% PEG4000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 28695 / % possible obs: 94.7 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.077 / Net I/σ(I): 12.2 |
Reflection shell | Resolution: 2.3→2.38 Å / Rmerge(I) obs: 0.318 / Mean I/σ(I) obs: 3.5 / % possible all: 80.9 |
-Processing
Software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1QPC Resolution: 2.3→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
| ||||||||||||||||||
Refine LS restraints |
|