CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2
The structure was published by Song, H., Hanlon, N., Brown, N.R., Noble, M.E., Johnson, L.N., and Barford, D., in 2001 in a paper entitled "Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely CYCLIN-DEPENDENT KINASE INHIBITOR 3 and CELL DIVISION PROTEIN KINASE 2.
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 most likely forms heterodimers.
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: