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- PDB-1a1c: C-SRC (SH2 DOMAIN) COMPLEXED WITH ACE-PHOSPHOTYR-GLU-(N-ME(-(CH2)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1a1c | ||||||
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Title | C-SRC (SH2 DOMAIN) COMPLEXED WITH ACE-PHOSPHOTYR-GLU-(N-ME(-(CH2)3-CYCLOPENTYL)) | ||||||
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![]() | COMPLEX (TRANSFERASE/PEPTIDE) / COMPLEX (TRANSFERASE-PEPTIDE) / COMPLEX (TRANSFERASE-PEPTIDE) complex | ||||||
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 | ![]() ![]() | ||||||
![]() | Shewchuk, L. / Jordan, S. | ||||||
![]() | ![]() Title: Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study. Authors: Charifson, P.S. / Shewchuk, L.M. / Rocque, W. / Hummel, C.W. / Jordan, S.R. / Mohr, C. / Pacofsky, G.J. / Peel, M.R. / Rodriguez, M. / Sternbach, D.D. / Consler, T.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.4 KB | Display | ![]() |
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PDB format | ![]() | 49.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1a07C ![]() 1a08C ![]() 1a09C ![]() 1a1aC ![]() 1a1bC ![]() 1a1eC ![]() 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.7933, 0.3005, -0.5295), Vector ![]() |
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Components
#1: Protein | ![]() Mass: 12303.886 Da / Num. of mol.: 2 / Fragment: SH2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 539.558 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 54 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 295 K / pH: 4.6 Details: PROTEIN WAS CRYSTALLIZED FROM 0.1 M ACETATE, PH 4.6,2M AMMONIUM SULFATE AT 22 C., temperature 295K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Mar 1, 1994 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.4→50 Å / Num. obs: 9865 / % possible obs: 91 % / Observed criterion σ(I): 1 / Redundancy: 3.2 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 11 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.178 / Mean I/σ(I) obs: 3.4 / % possible all: 83 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1SHD Resolution: 2.4→6 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0 / σ(F): 2 Details: PARTIALLY REFINED. NO SITE CHAIN DENSITY FOR THE FOLLOWING RESIDUES, THEREFORE MODELLED AS ALA: LYS A 184, ASN A 196, LYS A 198, GLN B 147, LYS B 155, ARG B 159, GLU B 169, LYS B 184, ASN B ...Details: PARTIALLY REFINED. NO SITE CHAIN DENSITY FOR THE FOLLOWING RESIDUES, THEREFORE MODELLED AS ALA: LYS A 184, ASN A 196, LYS A 198, GLN B 147, LYS B 155, ARG B 159, GLU B 169, LYS B 184, ASN B 196, LYS B 198, ASP B 211, LYS B 235. NO DENSITY VISIBLE FOR THE FOLLOWING RESIDUES, THEREFORE NOT INCLUDED IN THE MODEL: MET A 143, ASP A 144, MET B 143, ASP B 144, SER 145.
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Refinement step | Cycle: LAST / Resolution: 2.4→6 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: UNRESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.4→2.5 Å / Total num. of bins used: 8 / % reflection obs: 83 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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