Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure
The structure was published by Welburn, J.P.I., Tucker, J., Johnson, T., et al., Willis, A., Noble, M.E.M., and Endicott, J.A., in 2007 in a paper entitled "How Tyrosine 15 Phosphorylation Inhibits the Activity of Cyclin-Dependent Kinase 2-Cyclin A." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely CELL DIVISION PROTEIN KINASE 2 and CYCLIN A2.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 2 unique UniProt proteins: