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Open data
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Basic information
Entry | Database: PDB / ID: 2hy0 | ||||||
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Title | crystal structure of chek1 in complex with inhibitor 22 | ||||||
![]() | Serine/threonine-protein kinase Chk1 | ||||||
![]() | TRANSFERASE / Chek1 / Kinase / Cell cycle checkpoint | ||||||
Function / homology | ![]() negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination / negative regulation of gene expression, epigenetic ...negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination / negative regulation of gene expression, epigenetic / nucleus organization / cellular response to caffeine / Transcriptional Regulation by E2F6 / mitotic G2 DNA damage checkpoint signaling / Presynaptic phase of homologous DNA pairing and strand exchange / replicative senescence / signal transduction in response to DNA damage / Activation of ATR in response to replication stress / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / positive regulation of cell cycle / regulation of signal transduction by p53 class mediator / condensed nuclear chromosome / replication fork / DNA damage checkpoint signaling / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / TP53 Regulates Transcription of DNA Repair Genes / peptidyl-threonine phosphorylation / G2/M DNA damage checkpoint / Signaling by SCF-KIT / cellular response to mechanical stimulus / G2/M transition of mitotic cell cycle / regulation of cell population proliferation / Processing of DNA double-strand break ends / DNA replication / Regulation of TP53 Activity through Phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / chromatin remodeling / protein domain specific binding / protein phosphorylation / intracellular membrane-bounded organelle / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / apoptotic process / DNA damage response / chromatin / protein-containing complex / extracellular space / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yan, Y. | ||||||
![]() | ![]() Title: Development of 6-substituted indolylquinolinones as potent Chek1 kinase inhibitors. Authors: Huang, S. / Garbaccio, R.M. / Fraley, M.E. / Steen, J. / Kreatsoulas, C. / Hartman, G. / Stirdivant, S. / Drakas, B. / Rickert, K. / Walsh, E. / Hamilton, K. / Buser, C.A. / Hardwick, J. / ...Authors: Huang, S. / Garbaccio, R.M. / Fraley, M.E. / Steen, J. / Kreatsoulas, C. / Hartman, G. / Stirdivant, S. / Drakas, B. / Rickert, K. / Walsh, E. / Hamilton, K. / Buser, C.A. / Hardwick, J. / Mao, X. / Abrams, M. / Beck, S. / Tao, W. / Lobell, R. / Sepp-Lorenzino, L. / Yan, Y. / Ikuta, M. / Murphy, J.Z. / Sardana, V. / Munshi, S. / Kuo, L. / Reilly, M. / Mahan, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 73.5 KB | Display | ![]() |
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PDB format | ![]() | 53.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.7 KB | Display | ![]() |
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Full document | ![]() | 455.7 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 11.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hxlC ![]() 2hxqC ![]() 1ia8S 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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Unit cell |
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Components
#1: Protein | Mass: 36790.957 Da / Num. of mol.: 1 / Fragment: Chek1 kinase domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: O14757, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-306 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.78 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 13% PEG 8K, 0.1M ammonium sulfate, 2% glycerol, 0.1M cacodylate buffer at pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Dec 6, 2004 / Details: blue confocal optical system |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→37 Å / Num. all: 37452 / Num. obs: 36749 / % possible obs: 98 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Rmerge(I) obs: 0.063 / Rsym value: 0.063 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.374 / Mean I/σ(I) obs: 3.4 / Num. unique all: 3726 / Rsym value: 0.374 / % possible all: 82 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1IA8 Resolution: 1.7→37 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→37 Å
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Refine LS restraints |
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