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Open data
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Basic information
Entry | Database: PDB / ID: 1o4o | ||||||
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Title | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH PHENYLPHOSPHATE. | ||||||
![]() | PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC![]() | ||||||
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Function / homology | ![]() regulation of toll-like receptor 3 signaling pathway / positive regulation of non-membrane spanning protein tyrosine kinase activity / primary ovarian follicle growth / regulation of caveolin-mediated endocytosis / positive regulation of ovarian follicle development / cellular response to prolactin / positive regulation of platelet-derived growth factor receptor-beta signaling pathway / positive regulation of male germ cell proliferation / dendritic filopodium / regulation of cell projection assembly ...regulation of toll-like receptor 3 signaling pathway / positive regulation of non-membrane spanning protein tyrosine kinase activity / primary ovarian follicle growth / regulation of caveolin-mediated endocytosis / positive regulation of ovarian follicle development / cellular response to prolactin / positive regulation of platelet-derived growth factor receptor-beta signaling pathway / positive regulation of male germ cell proliferation / dendritic filopodium / regulation of cell projection assembly / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lange, G. / Loenze, P. / Liesum, A. | ||||||
![]() | ![]() Title: Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. Authors: Lange, G. / Lesuisse, D. / Deprez, P. / Schoot, B. / Loenze, P. / Benard, D. / Marquette, J.P. / Broto, P. / Sarubbi, E. / Mandine, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.5 KB | Display | ![]() |
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PDB format | ![]() | 25 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1o41C ![]() 1o42C ![]() 1o43C ![]() 1o44C ![]() 1o45C ![]() 1o46C ![]() 1o47C ![]() 1o48C ![]() 1o49C ![]() 1o4aC ![]() 1o4bC ![]() 1o4cC ![]() 1o4dC ![]() 1o4eC ![]() 1o4fC ![]() 1o4gC ![]() 1o4hC ![]() 1o4iC ![]() 1o4jC ![]() 1o4kC ![]() 1o4lC ![]() 1o4mC ![]() 1o4nC ![]() 1o4pC ![]() 1o4qC ![]() 1o4rC ![]() 1shdS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 12374.964 Da / Num. of mol.: 1 / Fragment: SH2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 41.9 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 5.5 / Details: pH 5.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.5 / Method: vapor diffusion, sitting drop / Details: Lesuisse, D., (2002) J.Med.Chem., 45, 2379. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Apr 22, 1998 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.7→40 Å / Num. obs: 11484 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.068 / Net I/σ(I): 15 |
Reflection shell | Resolution: 1.7→1.75 Å / Rmerge(I) obs: 0.206 / Mean I/σ(I) obs: 6 / % possible all: 94.1 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1SHD Resolution: 1.7→8 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.1
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Displacement parameters | Biso mean: 19.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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