HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160
The structure was published by Brown, N.R., Noble, M.E., Lawrie, A.M., et al., Divita, G., Johnson, L.N., and Endicott, J.A., in 1999 in a paper entitled "Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1998.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PROTEIN (CELL DIVISION PROTEIN KINASE 2). This molecule has the UniProt identifier P24941 (CDK2_HUMAN). The sample contained 299 residues which is 100% of the natural sequence. Out of 299 residues 291 were observed and are deposited in the PDB.
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 is most likely monomeric.
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 1 unique UniProt protein: