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- PDB-7r7k: Structure of Human Anaplastic Lymphoma Kinase Domain in complex w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7r7k | ||||||
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Title | Structure of Human Anaplastic Lymphoma Kinase Domain in complex with (4-[6-amino-5-[(1~{R})-1-[5-fluoro-2-(triazol-2-yl)phenyl]ethoxy]-3-pyridyl]isoindolin-1-one) | ||||||
![]() | ALK tyrosine kinase receptor | ||||||
![]() | TRANSFERASE / kinase | ||||||
Function / homology | ![]() ASP-3026-resistant ALK mutants / NVP-TAE684-resistant ALK mutants / alectinib-resistant ALK mutants / brigatinib-resistant ALK mutants / ceritinib-resistant ALK mutants / crizotinib-resistant ALK mutants / lorlatinib-resistant ALK mutants / MDK and PTN in ALK signaling / receptor signaling protein tyrosine kinase activator activity / regulation of dopamine receptor signaling pathway ...ASP-3026-resistant ALK mutants / NVP-TAE684-resistant ALK mutants / alectinib-resistant ALK mutants / brigatinib-resistant ALK mutants / ceritinib-resistant ALK mutants / crizotinib-resistant ALK mutants / lorlatinib-resistant ALK mutants / MDK and PTN in ALK signaling / receptor signaling protein tyrosine kinase activator activity / regulation of dopamine receptor signaling pathway / response to environmental enrichment / ALK mutants bind TKIs / swimming behavior / positive regulation of dendrite development / regulation of neuron differentiation / adult behavior / Signaling by ALK / neuron development / negative regulation of lipid catabolic process / energy homeostasis / peptidyl-tyrosine autophosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / transmembrane receptor protein tyrosine kinase activity / hippocampus development / receptor protein-tyrosine kinase / Signaling by ALK fusions and activated point mutants / positive regulation of NF-kappaB transcription factor activity / heparin binding / regulation of cell population proliferation / regulation of apoptotic process / protein tyrosine kinase activity / protein autophosphorylation / receptor complex / phosphorylation / signal transduction / protein-containing complex / extracellular exosome / ATP binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | McTigue, M. | ||||||
![]() | ![]() Title: Analysis of lorlatinib analogs reveals a roadmap for targeting diverse compound resistance mutations in ALK-positive lung cancer. Authors: Shiba-Ishii, A. / Johnson, T.W. / Dagogo-Jack, I. / Mino-Kenudson, M. / Johnson, T.R. / Wei, P. / Weinrich, S.L. / McTigue, M.A. / Walcott, M.A. / Nguyen-Phuong, L. / Dionne, K. / Acker, A. ...Authors: Shiba-Ishii, A. / Johnson, T.W. / Dagogo-Jack, I. / Mino-Kenudson, M. / Johnson, T.R. / Wei, P. / Weinrich, S.L. / McTigue, M.A. / Walcott, M.A. / Nguyen-Phuong, L. / Dionne, K. / Acker, A. / Kiedrowski, L.A. / Do, A. / Peterson, J.L. / Barth, J.L. / Yeap, B.Y. / Gainor, J.F. / Lin, J.J. / Yoda, S. / Hata, A.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.7 KB | Display | ![]() |
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PDB format | ![]() | 57.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 791.5 KB | Display | ![]() |
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Full document | ![]() | 792.1 KB | Display | |
Data in XML | ![]() | 15.2 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7r7rC ![]() 2xp2S S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 36909.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9UM73, receptor protein-tyrosine kinase |
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#2: Chemical | ChemComp-25J / |
#3: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.84 % |
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Crystal grow | Temperature: 286 K / Method: vapor diffusion, hanging drop Details: HANGING DROP VAPOR DIFFUSION AT 13 DEGREES C. EQUAL VOLUMES OF PURIFIED PROTEIN SOLUTION(APPROXIMATELY 13-15 MG/ML)CONTAINING 0.0011M INHIBITOR COMPOUND WERE COMBINED WITH A SOLUTION ...Details: HANGING DROP VAPOR DIFFUSION AT 13 DEGREES C. EQUAL VOLUMES OF PURIFIED PROTEIN SOLUTION(APPROXIMATELY 13-15 MG/ML)CONTAINING 0.0011M INHIBITOR COMPOUND WERE COMBINED WITH A SOLUTION CONTAINING: 0.15M AMMONIUM SULFATE, 9-10.5% MONOMETHYLETHER PEG5K AND 0.1M MES IN THE PH RANGE 5.3-6.5 |
-Data collection
Diffraction | Mean temperature: 87 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 23, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.83→52.72 Å / Num. obs: 28124 / % possible obs: 99.4 % / Redundancy: 6.5 % / Rmerge(I) obs: 0.057 / Rpim(I) all: 0.026 / Net I/σ(I): 23.3 |
Reflection shell | Resolution: 1.83→1.93 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.47 / Num. unique obs: 4020 / Rpim(I) all: 0.211 / % possible all: 98.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2xp2 Resolution: 1.831→52.72 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.922 / SU R Cruickshank DPI: 0.135 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.146 / SU Rfree Blow DPI: 0.128 / SU Rfree Cruickshank DPI: 0.122
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Displacement parameters | Biso mean: 27.76 Å2
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Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.831→52.72 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.831→1.84 Å
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