2C6M
Crystal structure of the human CDK2 complexed with the triazolopyrimidine inhibitor
Summary for 2C6M
Entry DOI | 10.2210/pdb2c6m/pdb |
Related | 1AQ1 1B38 1B39 1BUH 1CKP 1DI8 1DM2 1E1V 1E1X 1E9H 1F5Q 1FIN 1FQ1 1FVT 1FVV 1G5S 1GIH 1GII 1GIJ 1GY3 1GZ8 1H00 1H01 1H07 1H08 1H0V 1H0W 1H1P 1H1Q 1H1R 1H1S 1H24 1H25 1H26 1H27 1H28 1HCK 1HCL 1JST 1JSU 1JSV 1JVP 1KE5 1KE6 1KE7 1KE8 1KE9 1OGU 1OI9 1OIQ 1OIR 1OIT 1OIU 1OIY 1OKU 1OKV 1OKW 1OL1 1OL2 1P2A 1P5E 1PF8 1PKD 1PW2 1PXI 1PXJ 1PXK 1PXL 1PXM 1PXN 1PXO 1PXP 1PYE 1QMZ 1R78 1URC 1URW 1V1K 1VYW 1VYZ 1W0X 1W8C 1W98 1WCC 1Y8Y 1Y91 2B52 2B53 2B54 2B55 2BHE 2BHH 2BKZ 2BPM 2BTR 2BTS 2C4G 2C5N 2C5O 2C5P 2C5T 2C5V 2C5X 2C5Y 2C68 2C69 2C6I 2C6K 2C6L 2C6O 2C6T |
Descriptor | CELL DIVISION PROTEIN KINASE 2, 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE (3 entities in total) |
Functional Keywords | transferase, serine/threonine protein kinase, cdk2, atp-binding, cell cycle, mitosis, phosphorylation, triazolopyrimidine inhibitor, cell division, kinase, polymorphism, nucleotide-binding |
Biological source | HOMO SAPIENS (HUMAN) |
Total number of polymer chains | 1 |
Total formula weight | 34364.93 |
Authors | Richardson, C.M.,Dokurno, P.,Murray, J.B.,Surgenor, A.E. (deposition date: 2005-11-10, release date: 2005-12-07, Last modification date: 2023-12-13) |
Primary citation | Richardson, C.M.,Williamson, D.S.,Parratt, M.J.,Borgognoni, J.,Cansfield, A.D.,Dokurno, P.,Francis, G.L.,Howes, R.,Moore, J.D.,Murray, J.B.,Robertson, A.,Surgenor, A.E.,Torrance, C.J. Triazolo[1,5-A]Pyrimidines as Novel Cdk2 Inhibitors: Protein Structure-Guided Design and Sar. Bioorg.Med.Chem.Lett., 16:1353-, 2006 Cited by PubMed Abstract: Crystallographic and modelling data, in conjunction with a medicinal chemistry template-hopping approach, led to the identification of a series of novel and potent inhibitors of human cyclin-dependent kinase 2 (CDK2), with selectivity over glycogen synthase kinase-3beta (GSK-3beta). One example had a CDK2 IC(50) of 120 nM and showed selectivity over GSK-3beta of 167-fold. PubMed: 16325401DOI: 10.1016/J.BMCL.2005.11.048 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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