This superfamily includes the glycerophosphodiesterase (GDPD) from Enterobacter aerogenes, GpdQ, a promiscuous binuclear metallohydrolase that belongs to a diverse family of metallo-phosphoesterases. It plays a role in catalysing the hydrolysis of mono-, di- and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents.

This entry represents the dimerisation domain of GpdQ, consisting of a pair of two-stranded antiparallel beta-sheets and a short beta-strand in the loop between the sheets, from each subunit, joining the beta-sandwiches from each subunit. A disjointed single beta-sandwich is formed across the length of the dimer. The fold of this domain consists of a pair of two-stranded beta-sheets from each chain, longer than the beta-sheets from the alpha/beta sandwich domain, with a shorter third strand from each chain not directly contributing to the dimer interface.

DOI:10.1016/j.jmb.2007.01.032,DOI:10.1021/ja803346w