2XCK

Crystal structure of PDK1 in complex with a pyrazoloquinazoline inhibitor

Summary for 2XCK

Entry DOI	10.2210/pdb2xck/pdb
Related	1H1W 1OKY 1OKZ 1UU3 1UU7 1UU8 1UU9 1UVR 1W1D 1W1G 1W1H 1Z5M 2BIY 2VKI 2XCH
Descriptor	3-PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1, 1-METHYL-8-{[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]AMINO}-N-[(2-METHYLPYRIDIN-4-YL)METHYL]-4,5-DIHYDRO-1H-PYRAZOLO[4,3-H]QUINAZOLINE-3-CARBOXAMIDE, GLYCEROL, ... (5 entities in total)
Functional Keywords	pi3-kinase signalling, transferase, atp-binding, serine/threonine-protein kinase
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cytoplasm: O15530
Total number of polymer chains	1
Total formula weight	36609.78
Authors	Angiolini, M.,Banfi, P.,Casale, E.,Casuscelli, F.,Fiorelli, C.,Saccardo, M.B.,Silvagni, M.,Zuccotto, F. (deposition date: 2010-04-23, release date: 2010-07-28, Last modification date: 2024-10-16)
Primary citation	Angiolini, M.,Banfi, P.,Casale, E.,Casuscelli, F.,Fiorelli, C.,Saccardo, M.B.,Silvagni, M.,Zuccotto, F. Structure-Based Optimization of Potent Pdk1 Inhibitors. Bioorg.Med.Chem.Lett., 20:4095-, 2010 Cited by PubMed Abstract: In this Letter is described the structure-based design of potent dihydro-pyrazoloquinazolines as PDK1 inhibitors. Starting from low potency HTS hits with the aid of X-ray crystallography and modeling, a medicinal chemistry activity was carried out to improve potency versus PDK1 and selectivity versus CDK2 protein kinase. PubMed: 20621725 DOI: 10.1016/J.BMCL.2010.05.070 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation