The N-terminal domain has a multi-helical structure that can be divided into two subdomains.

Their N-terminal domains, however, exhibit a large degree of variance in the size and sequence.

The other domain (N-terminal domain) is not known to have any function.

Only the N-terminal domain appears to be enzymatically active.

When they interact, the conformation of the N-terminal domain is changed so as to open the pore.

The N-terminal domain is smaller in size but far more rich in selenium.

The N-terminal domain is thought to be part of the functional domain.

The N-terminal domain folds into two alpha-helices and one beta-strand.

There are eight alpha helices that form the N-terminal domain.

The globular end of each subunit are identical and is the N-terminal domain.