Crystal structure of Fus3 with a docking motif from Msg5
The structure was published by Remenyi, A., Good, M.C., Bhattacharyya, R.P., and Lim, W.A., in 2005 in a paper entitled "The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Mitogen-activated protein kinase FUS3 and Tyrosine-protein phosphatase MSG5.
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 most likely forms heterodimers.
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: