<p> Peptidylglycine alpha-hydroxylating monooxygenase (PHM) is a copper-containing enzyme that catalyses an oxygen-dependent hydroxylation of peptide-extended glycine residues. Members of this family bind peptide substrates and consists of two domains of this fold packed together. Structurally, this domain consists of a beta-sandwich of 8 strands in 2 beta-sheets, in a jelly-roll topology [<cite idref="PUB00011821"/>].This domain can also be found in the enzyme Peptide:N-glycosidase F (PNGase F), which catalyses the complete removal of N-linked oligosaccharide chains from glycoproteins [<cite idref="PUB00035451"/>].</p> PHM/PNGase F-fold domain