1E9H

Thr 160 phosphorylated CDK2 - Human cyclin A3 complex with the inhibitor indirubin-5-sulphonate bound

Summary for 1E9H

• Entry DOI: 10.2210/pdb1e9h/pdb
• Related: 1AQ1 1B38 1B39 1CKP 1DM2 1E1V 1E1X 1FIN 1HCK 1HCL 1JST 1JSU 1QMZ
• Descriptor: CELL DIVISION PROTEIN KINASE 2, CYCLIN A3, 2',3-DIOXO-1,1',2',3-TETRAHYDRO-2,3'-BIINDOLE-5'-SULFONIC ACID, ... (4 entities in total)
• Functional Keywords: cell cycle, complex (protein kinase-cyclin), kinases, inhibitor, cyclin, complex, phosphorylation
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: P20248
• Total number of polymer chains: 4
• Total formula weight: 128360.47

Authors

Davies, T.G.,Tunnah, P.,Noble, M.E.M.,Endicott, J.A. (deposition date: 2000-10-16, release date: 2001-10-11, Last modification date: 2024-11-13)

Primary citation

Davies, T.G.,Tunnah, P.,Meijer, L.,Marko, D.,Eisenbrand, G.,Endicott, J.A.,Noble, M.E.
Inhibitor Binding to Active and Inactive Cdk2: The Crystal Structure of Cdk2-Cyclin A/Indirubin-5-Sulphonate
Structure, 9:389-, 2001

PubMed Abstract: Cyclin-dependent kinase 2 (CDK2) is an important target for structure-based design of antitumor agents. Monomeric CDK2 is inactive. Activation requires rearrangements to key structural elements of the enzyme's active site, which accompany cyclin binding and phosphorylation. To assess the validity of using monomeric CDK2 as a model for the active kinase in structure-based drug design, we have solved the structure of the inhibitor indirubin-5-sulphonate (E226) complexed with phospho-CDK2-cyclin A and compared it with the structure of E226 bound to inactive, monomeric CDK2.

PubMed: 11377199
DOI: 10.1016/S0969-2126(01)00598-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)