The prostaglandin H synthase structure reveals that the enzyme has a f
old similar to those of other heme peroxidases, but differing in that
a second active site has evolved within this fold which catalyzes the
cyclooxygenase reaction. The protein has also acquired two additional
domains: a membrane-binding motif that lacks transmembrane segments, m
ediating attachment to the membrane via helices that lie parallel to t
he membrane, and an epidermal growth factor-like module found just bef
ore the membrane-binding motif. The epidermal growth factor-like modul
e is located in the dimer interface.