The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer being comprised of two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed β-pleated sheet and five α-helices, which are arranged on the external surface of the β-sheet. This, in turn, faces the β-sheet of the C-terminal … expand

The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer being comprised of two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed β-pleated sheet and five α-helices, which are arranged on the external surface of the β-sheet. This, in turn, faces the β-sheet of the C-terminal subdomain to form a double β-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains [ PUBMED:10673422 ]. In humans, deficiency of this enzyme results in a disease phenotype [ PUBMED:12815595 ].

This entry represents the C-terminal subdomain of the formiminotransferase domain.