The active site heme, however, is uniquely ligated by a single lysine residue.

The essential lysine residue in the active site plays an important role in regulation of activity.

Its lysine residue, at position 51, also has a special feature: it interacts with mammalian Na channels.

Other posttranslational modifications at lysine residues include acetylation and ubiquitination.

Neutravidin still has lysine residues that remain available for derivatization or conjugation.

Key features include its C-terminal tail and the 7 lysine residues.

As discussed, ubiquitin possesses a total of 7 lysine residues.

The pyridoxal-P group is attached to a lysine residue located in the central section of these enzymes.

Approximately nine of the 30 lysine residues in each chain are pegylated.

However, the A subunit lacks lysine residues, which are essential for ubiquitin-dependent degradation.