THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4-[3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE
The structure was published by Shewchuk, L., Hassell, A., Wisely, B., et al., Holmes, W., Veal, J., and Kuyper, L.F., in 2000 in a paper entitled "Binding mode of the 4-anilinoquinazoline class of protein kinase inhibitor: X-ray crystallographic studies of 4-anilinoquinazolines bound to cyclin-dependent kinase 2 and p38 kinase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1999.
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 281 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: