The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:"
Available structural information on PhDph2 reveals that this enzyme is a homodimer and that each monomer comprises three domains which share the same overall fold. The basic domain fold is a four-stranded parallel beta-sheet with three flanking alpha-helices (or two alpha-helices and one 3(10) helix in the case of domain 2). The two beta-sheets in domain 1 and 2 each contain an additional beta-strand that is antiparallel to the rest of the beta-sheet. Domains 2 and 3 have two additional alpha-helices. Domain 1 of one monomer and domain 3 of the adjacent monomer form the dimer interface, creating an extended nine-stranded beta-sheet. The domain folds and their arrangement resemble the structure of quinolinate synthase but the orientations of the domains with respect to each other are different in the two enzymes. Three conserved cysteine residues (Cys59, Cys163 and Cys287), each coming from a different structural domain, are clustered together in the center of the PhDph2 monomers. All three cysteine residues are conserved in eukaryotic DPH1s. The first and third cysteine residues are conserved in eukaryotic DPH2s PMID:20559380.
|Domain clusters (>95% seq id):||1|
|Domain clusters (>35% seq id):||1|
|Structural Clusters (5A):||1|
|Structural Clusters (9A):||1|