Zinc fingers AN1-type
zinc fingers an1-type
In molecular biology, the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1, a ubiquitin-like protein in Xenopus laevis. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms.