Crystal structure of Fus3 phosphorylated on Tyr182
The structure was published by Bhattacharyya, R.P., Remenyi, A., Good, M.C., Bashor, C.J., Falick, A.M., and Lim, W.A., in 2006 in a paper entitled "The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Mitogen-activated protein kinase FUS3. This molecule has the UniProt identifier P16892 (FUS3_YEAST). The sample contained 353 residues which is 100% of the natural sequence. Out of 353 residues 328 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: