CRYSTAL STRUCTURE OF DI-PHOSPHORYLATED HUMAN CLK1 IN COMPLEX WITH A NOVEL SUBSTITUTED INDOLE INHIBITOR
The structure was published by Fedorov, O., Huber, K., Eisenreich, A., et al., Rauch, U., Bracher, F., and Knapp, S., in 2011 in a paper entitled "Specific Clk Inhibitors from a Novel Chemotype for Regulation of Alternative Splicing." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of DUAL SPECIFICITY PROTEIN KINASE CLK1. This molecule has the UniProt identifier P49759 (CLK1_HUMAN). The sample contained 339 residues which is < 90% of the natural sequence. Out of 339 residues 321 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: