v5.1.0.3
Glycine data from LIS
Type | Homologous_superfamily |
Description | Dimeric α-β barrel domains exhibit an α+β sandwich fold with an antiparallel β-sheet that forms a closed barrel. These domains dimerise through the β-sheet, and in some cases these dimers may assemble into higher oligomers. Domains with this structure are found in proteins from several different families, including bacterial actinorhodin biosynthesis monooxygenase (ActVa-Orf6), which catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway [ ]; bacterial muconalactone isomerase, a decamer composed of five dimers []; and the C-terminal domain of archaeal LprA, a member of the Lrp/AqsnC family of transcription regulators []. |
Short Name | Dimeric_a/b-barrel |