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- PDB-4omp: Crystal structure of the intertwined dimer of the c-Src tyrosine ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4omp | ||||||
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Title | Crystal structure of the intertwined dimer of the c-Src tyrosine kinase SH3 domain mutant Q128K | ||||||
![]() | Proto-oncogene tyrosine-protein kinase Src | ||||||
![]() | TRANSFERASE / beta-barrel sandwich / kinase / proline rich motifs | ||||||
Function / homology | ![]() Signaling by ERBB2 / Nuclear signaling by ERBB4 / PIP3 activates AKT signaling / Signaling by SCF-KIT / Regulation of KIT signaling / Signaling by EGFR / GAB1 signalosome / Regulation of gap junction activity / FCGR activation / PECAM1 interactions ...Signaling by ERBB2 / Nuclear signaling by ERBB4 / PIP3 activates AKT signaling / Signaling by SCF-KIT / Regulation of KIT signaling / Signaling by EGFR / GAB1 signalosome / Regulation of gap junction activity / FCGR activation / PECAM1 interactions / CD28 co-stimulation / CTLA4 inhibitory signaling / EPHA-mediated growth cone collapse / Ephrin signaling / G alpha (i) signalling events / GP1b-IX-V activation signalling / Thrombin signalling through proteinase activated receptors (PARs) / VEGFR2 mediated cell proliferation / RAF activation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RET signaling / Receptor Mediated Mitophagy / ADP signalling through P2Y purinoceptor 1 / Downregulation of ERBB4 signaling / EPH-ephrin mediated repulsion of cells / Cyclin D associated events in G1 / Regulation of RUNX3 expression and activity / Activated NTRK3 signals through PI3K / Downstream signal transduction / MAP2K and MAPK activation / Integrin signaling / GRB2:SOS provides linkage to MAPK signaling for Integrins / DCC mediated attractive signaling / MET activates PTK2 signaling / Extra-nuclear estrogen signaling / EPHB-mediated forward signaling / p130Cas linkage to MAPK signaling for integrins / VEGFA-VEGFR2 Pathway / connexin binding / osteoclast development / progesterone receptor signaling pathway / negative regulation of intrinsic apoptotic signaling pathway / bone resorption / extrinsic component of cytoplasmic side of plasma membrane / negative regulation of extrinsic apoptotic signaling pathway / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / epidermal growth factor receptor signaling pathway / cell junction / protein phosphatase binding / protein tyrosine kinase activity / mitochondrial inner membrane / cell differentiation / cytoskeleton / endosome membrane / cell adhesion / regulation of cell cycle / cell cycle / phosphorylation / innate immune response / focal adhesion / signaling receptor binding / heme binding / perinuclear region of cytoplasm / protein-containing complex / ATP binding / membrane / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Camara-Artigas, A. / Bacarizo, J. | ||||||
![]() | ![]() Title: Electrostatic Effects in the Folding of the SH3 Domain of the c-Src Tyrosine Kinase: pH-Dependence in 3D-Domain Swapping and Amyloid Formation. Authors: Bacarizo, J. / Martinez-Rodriguez, S. / Martin-Garcia, J.M. / Andujar-Sanchez, M. / Ortiz-Salmeron, E. / Neira, J.L. / Camara-Artigas, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 26.3 KB | Display | ![]() |
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PDB format | ![]() | 15.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.1 KB | Display | ![]() |
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Full document | ![]() | 439.1 KB | Display | |
Data in XML | ![]() | 4.4 KB | Display | |
Data in CIF | ![]() | 5.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4jz3C ![]() 4jz4SC ![]() 4omlC ![]() 4omnC ![]() 4omoC C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 8593.474 Da / Num. of mol.: 1 / Fragment: SH3 domain / Mutation: Q128K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00523, non-specific protein-tyrosine kinase |
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#2: Chemical | ChemComp-PGE / |
#3: Chemical | ChemComp-PEG / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.83 % |
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Crystal grow | Temperature: 298 K / pH: 5 Details: 0.1M sodium acetate, 1.8 M ammonium sulphate, 5% PEG 300, 10%Glicerol, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||
Detector | Type: PILATUS 6M (DECTRIS) / Detector: CCD / Date: Jul 11, 2012 / Details: CHANNEL-CUT SI(111) + KB FOCUSING MIRRORS | ||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||
Radiation wavelength | Wavelength: 0.979505 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Redundancy: 11.7 % / Number: 70435 / Rmerge(I) obs: 0.056 / D res high: 2 Å / D res low: 29.39 Å / Num. obs: 6002 / % possible obs: 98.6 | ||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 2→29.39 Å / Num. obs: 6002 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 11.7 % / Biso Wilson estimate: 36.96 Å2 / Rmerge(I) obs: 0.056 / Rsym value: 23.4 / Net I/σ(I): 23.4 | ||||||||||||||||||
Reflection shell | Resolution: 2→2.06 Å / Redundancy: 11.5 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 4.9 / % possible all: 96.3 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4JZ4 Resolution: 2→29.39 Å / SU ML: 0.37 / Isotropic thermal model: isotropic / σ(F): 1.54 / Phase error: 37.98 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.46 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→29.39 Å
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Refine LS restraints |
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LS refinement shell |
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