The ring is formed by a disulfide bond between two cysteine residues at positions 7 and 23.

They have a nearly identical placement of cysteine residues and glycosylation sites.

Finally, a disulfide bond is formed between cysteine residues numbers 2 and 7.

It contains four cysteine residues that form two disulphide bonds.

Having 6 cysteine residues, the oxidation state has a significant effect on the protein structure.

Several conserved cysteine residues are present at positions 226,235, 335, 364,449, 581, 675, 925, and 985.

Another feature of these sequences is the conservation of cysteine residues.

Their alignments also highlight the conservation of the cysteine residues that we describe in Fig.

CCN1 has unusually high cysteine residue content (10% or 38 in total).

There are two conserved cysteine residues important for thiolase activity.