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My protein, lymphoid tyrosine phosphatase (LYP) is composed of alpha helixes and beta pleated sheets. Having only one unit, and no subunits, this protein has no quaternary structure. An important protein in the function of the human autoimmune system, LYP is a target for modern drugs and possesses a large risk factor. Recent studies of the structure of this protein have revealed a rather unusual disulfide bond between the catalytic CYS and a local non-catalytic CYS. This disulfide bond is important to the regulatory function of LYP. The study also found a phosphate ion bonded in the active center of LYP which, upon dephosphorylation but before the actual release of the phosphate, the protein will take on an intermediate conformation. These finds help us understand more about the regulation of this protein, which in turn helps us find out more about the human immune system.