|Entry||Database: PDB / ID: 1h08|
|Title||CDK2 in complex with a disubstituted 2, 4-bis anilino pyrimidine CDK4 inhibitor|
|Components||CELL DIVISION PROTEIN KINASE 2|
|Keywords||TRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / MITOSIS|
|Function / homology|
Function and homology information
Orc1 removal from chromatin / G0 and Early G1 / Activation of ATR in response to replication stress / Regulation of APC/C activators between G1/S and early anaphase / SCF(Skp2)-mediated degradation of p27/p21 / Senescence-Associated Secretory Phenotype (SASP) / DNA Damage/Telomere Stress Induced Senescence / Processing of DNA double-strand break ends / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Regulation of TP53 Degradation ...Orc1 removal from chromatin / G0 and Early G1 / Activation of ATR in response to replication stress / Regulation of APC/C activators between G1/S and early anaphase / SCF(Skp2)-mediated degradation of p27/p21 / Senescence-Associated Secretory Phenotype (SASP) / DNA Damage/Telomere Stress Induced Senescence / Processing of DNA double-strand break ends / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Regulation of TP53 Degradation / G2 Phase / Regulation of TP53 Activity through Phosphorylation / Activation of the pre-replicative complex / Factors involved in megakaryocyte development and platelet production / Meiotic recombination / PTK6 Regulates Cell Cycle / CDK-mediated phosphorylation and removal of Cdc6 / Cyclin A:Cdk2-associated events at S phase entry / p53-Dependent G1 DNA Damage Response / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin E associated events during G1/S transition / Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cyclin A1-CDK2 complex / cyclin A2-CDK2 complex / positive regulation of DNA-dependent DNA replication initiation / Y chromosome / cyclin-dependent protein kinase activity / X chromosome / histone phosphorylation / centrosome duplication / centriole replication / cyclin-dependent kinase / cyclin-dependent protein serine/threonine kinase activity / cyclin-dependent protein kinase holoenzyme complex / condensed chromosome / Cajal body / cellular response to nitric oxide / mitotic G1 DNA damage checkpoint / cyclin binding / regulation of gene silencing / potassium ion transport / meiotic cell cycle / chromosome, telomeric region / G1/S transition of mitotic cell cycle / regulation of G2/M transition of mitotic cell cycle / anaphase-promoting complex-dependent catabolic process / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / Ras protein signal transduction / transcription factor complex / G2/M transition of mitotic cell cycle / regulation of signal transduction by p53 class mediator / DNA replication / endosome / peptidyl-serine phosphorylation / centrosome / cell division / DNA repair / protein domain specific binding / protein serine/threonine kinase activity / protein phosphorylation / positive regulation of cell population proliferation / positive regulation of transcription, DNA-templated / magnesium ion binding / negative regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain profile. / Protein kinase-like domain superfamily / Protein kinase domain / Protein kinase, ATP binding site / Protein kinase domain / Protein kinases ATP-binding region signature.
Cyclin-dependent kinase 2
|Biological species||HOMO SAPIENS (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å|
|Authors||Breault, G.A. / Ellston, R.P.A. / Green, S. / James, S.R. / Jewsbury, P.J. / Midgley, C.J. / Minshull, C.A. / Pauptit, R.A. / Tucker, J.A. / Pease, J.E.|
Journal: Bioorg.Med.Chem.Lett. / Year: 2003
Title: Cyclin-Dependent Kinase 4 Inhibitors as a Treatment for Cancer. Part 1: Identification and Optimisation of Substituted 4,6-Bis Anilino Pyrimidines
Authors: Beattie, J.F. / Breault, G.A. / Ellston, R.P.A. / Green, S. / Jewsbury, P.J. / Midgley, C.J. / Naven, R.T. / Minshull, C.A. / Pauptit, R.A. / Tucker, J.A. / Pease, J.E.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: CELL DIVISION PROTEIN KINASE 2
|#1: Protein/peptide|| |
Mass: 34002.527 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / Strain (production host): SF9 / References: UniProt: P24941, EC: 18.104.22.168
|#2: Chemical|| ChemComp-BYP / (|
|#3: Chemical|| ChemComp-BWP / (|
|#4: Chemical|| ChemComp-GOL / |
|#5: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2 Å3/Da / Density % sol: 38 %|
|Crystal grow||pH: 7 |
Details: PROTEIN AT 10MG/ML WELL BUFFER CONTAINING 17.5% PEG3350, 200MM HEPES, PH7.0, 100MM AMMONIUM ACETATE, pH 7.00
*PLUSMethod: unknown / Details: Lawrie, A.M., (1997) Nat.Struct.Biol., 4, 796.
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.93|
|Detector||Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 15, 1998 / Details: SAGITALLY FOCUSSING GE (220)|
|Radiation||Monochromator: DIAMOND (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.93 Å / Relative weight: 1|
|Reflection||Resolution: 1.79→36.78 Å / Num. obs: 26414 / % possible obs: 99.5 % / Redundancy: 4.1 % / Biso Wilson estimate: 23.9 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 18.5|
|Reflection shell||Resolution: 1.79→1.89 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.455 / Mean I/σ(I) obs: 2.3 / % possible all: 99.7|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→36.78 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1223590.24 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 |
Details: RESIDUES 36 - 43 AND 154 - 160 ARE NOT VISIBLE IN THE ELECTRON DENSITY MAP
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 48.5559 Å2 / ksol: 0.358635 e/Å3|
|Displacement parameters||Biso mean: 33.7 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.8→36.78 Å|
|Refine LS restraints|
Refinement-ID: X-RAY DIFFRACTION
|LS refinement shell||Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 6 |
Refinement-ID: X-RAY DIFFRACTION
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