2OXD
Protein kinase CK2 in complex with tetrabromobenzoimidazole K17, K22 and K32 inhibitors
Summary for 2OXD
| Entry DOI | 10.2210/pdb2oxd/pdb |
| Related | 1j91 1zoe 1zog 1zoh 2OXX 2OXY |
| Descriptor | Casein kinase II subunit alpha, 4,5,6,7-TETRABROMO-1H,3H-BENZIMIDAZOL-2-ONE (3 entities in total) |
| Functional Keywords | kinase, inhibitor complex, transferase |
| Biological source | Zea mays |
| Total number of polymer chains | 1 |
| Total formula weight | 39740.88 |
| Authors | Battistutta, R.,Zanotti, G.,Cendron, L. (deposition date: 2007-02-20, release date: 2007-09-25, Last modification date: 2023-08-30) |
| Primary citation | Battistutta, R.,Mazzorana, M.,Cendron, L.,Bortolato, A.,Sarno, S.,Kazimierczuk, Z.,Zanotti, G.,Moro, S.,Pinna, L.A. The ATP-Binding Site of Protein Kinase CK2 Holds a Positive Electrostatic Area and Conserved Water Molecules. Chembiochem, 8:1804-1809, 2007 Cited by PubMed Abstract: CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity. PubMed: 17768728DOI: 10.1002/cbic.200700307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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