Crystal structure of human CDK2 in complex with the inhibitor olomoucine.
The structure was published by Schulze-Gahmen, U., Brandsen, J., Jones, H.D., et al., Meijer, L., Vesely, J., and Kim, S.H., in 1995 in a paper entitled "Multiple Modes of Ligand Recognition: Crystal Structures of Cyclin-Dependent Protein Kinase 2 in Complex with ATP and Two Inhibitors, Olomoucine and Isopentenyladenine." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of CYCLIN-DEPENDENT KINASE 2. This molecule has the UniProt identifier P24941 (CDK2_HUMAN). The sample contained 298 residues which is 100% of the natural sequence. Out of 298 residues 279 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: