This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is acylphosphate phosphohydrolase. Other names in common use include acetylphosphatase, 1,3-diphosphoglycerate phosphatase, acetic phosphatase, Ho 1-3, and GP 1-3.
Structures of this enzyme have been solved by both NMR and X-ray crystallography. See the links to PDB structures in the info boxes on the right for a current list of structures available in the PDB. The protein contains a beta sheet stacked on two alpha helices described by CATH as an Alpha-Beta Plait fold. The active site sits between sheet and helices and contains an arginine and an asparagine.  Most structures are monomeric 
^Pastore A, Saudek V, Ramponi G, Williams RJ (March 1992). "Three-dimensional structure of acylphosphatase. Refinement and structure analysis". J. Mol. Biol.224 (2): 427–40. doi:10.1016/0022-2836(92)91005-A. PMID1313885.
^Stefani M, Taddei N, Ramponi G (February 1997). "Insights into acylphosphatase structure and catalytic mechanism". Cell. Mol. Life Sci.53 (2): 141–51. doi:10.1007/PL00000585. PMID9118002.
^Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Gribenko et al PNAS 2009. PMID 19196981.