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- PDB-1u54: Crystal Structures of the Phosphorylated and Unphosphorylated Kin... -
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Basic information
Entry | Database: PDB / ID: 1u54 | ||||||
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Title | Crystal Structures of the Phosphorylated and Unphosphorylated Kinase Domains of the CDC42-associated Tyrosine Kinase ACK1 bound to AMP-PCP | ||||||
![]() | (Activated CDC42 kinase 1) x 2 | ||||||
![]() | TRANSFERASE / Tyrosine Kinase | ||||||
Function / homology | ![]() regulation of clathrin-dependent endocytosis / regulation of keratinocyte differentiation / Grb2-EGFR complex / GTPase inhibitor activity / cytoophidium / WW domain binding / clathrin-coated vesicle / epidermal growth factor receptor binding / small GTPase-mediated signal transduction / negative regulation of epidermal growth factor receptor signaling pathway ...regulation of clathrin-dependent endocytosis / regulation of keratinocyte differentiation / Grb2-EGFR complex / GTPase inhibitor activity / cytoophidium / WW domain binding / clathrin-coated vesicle / epidermal growth factor receptor binding / small GTPase-mediated signal transduction / negative regulation of epidermal growth factor receptor signaling pathway / clathrin-coated pit / protein serine/threonine/tyrosine kinase activity / adherens junction / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / cytoplasmic vesicle membrane / endocytosis / positive regulation of peptidyl-tyrosine phosphorylation / protein tyrosine kinase activity / cell surface receptor signaling pathway / non-specific serine/threonine protein kinase / endosome / phosphorylation / intracellular membrane-bounded organelle / protein serine kinase activity / protein serine/threonine kinase activity / ubiquitin protein ligase binding / perinuclear region of cytoplasm / ATP binding / identical protein binding / membrane / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lougheed, J.C. / Chen, R.H. / Mak, P. / Stout, T.J. | ||||||
![]() | ![]() Title: Crystal Structures of the Phosphorylated and Unphosphorylated Kinase Domains of the Cdc42-associated Tyrosine Kinase ACK1. Authors: Lougheed, J.C. / Chen, R.H. / Mak, P. / Stout, T.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.6 KB | Display | ![]() |
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PDB format | ![]() | 92.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 22.3 KB | Display | |
Data in CIF | ![]() | 29.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1u46SC ![]() 1u4dC 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33138.023 Da / Num. of mol.: 1 / Fragment: Kinase Domain Source method: isolated from a genetically manipulated source Details: phosphorylated at residue 284 / Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 33058.047 Da / Num. of mol.: 1 / Fragment: Kinase Domain Source method: isolated from a genetically manipulated source Details: unphosphorylated at residue 284 / Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-MG / #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 45.2 % |
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Crystal grow | Temperature: 291 K / pH: 8.5 Details: PEG 4000, lithium sulfate, magnesium chloride, sodium chloride, AMP-PCP, Tris, TCEP, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K, pH 8.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 21, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.954 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→38.71 Å / Num. obs: 14697 / % possible obs: 98.3 % / Redundancy: 3.6 % / Rsym value: 0.058 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 3.64 % / Mean I/σ(I) obs: 3.7 / Rsym value: 0.319 / % possible all: 97.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1U46 Resolution: 2.8→38.71 Å / Cor.coef. Fo:Fc: 0.916 / Cor.coef. Fo:Fc free: 0.842 / SU B: 19.96 / SU ML: 0.396 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.51 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS, TLS REFINEMENT WAS USED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.15 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→38.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.87 Å / Total num. of bins used: 20 /
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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