Structure of the Catalytic Domain of Human Polo-like Kinase 1
The structure was published by Kothe, M., Kohls, D., Low, S., et al., Wynn, T.A., Kuhn, C., and Ding, Y.H., in 2007 in a paper entitled "Structure of the catalytic domain of human polo-like kinase 1." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Serine/threonine-protein kinase PLK1. This molecule has the UniProt identifier P53350 (PLK1_HUMAN). The sample contained 335 residues which is < 90% of the natural sequence. Out of 335 residues 294 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 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 1 unique UniProt protein: