A structural model for the active site of phosphoesterases, enzymes that degrade organophosphate neurotoxins, has been synthesised. The ligand [2-((2-hydroxy-3-(((2-hydroxyethyl)(pyridin-2-ylmethyl)amino)methyl) -5-methylbenzyl)(pyridin-2-ylmethyl)amino)acetic acid] (H3L1) and two Zn(ii) complexes have been prepared and characterised as [Zn 2(HL1)(CH3COO)](PF6)·H2O and Li[Zn2(HL1)]4(PO4)2(PF 6)3·(CH3OH). The ligand (H 3L1) and complex [Zn2(HL1)(CH3COO)](PF 6)·H2O were characterised through 1H NMR, 13C NMR, mass spectroscopy and microanalysis. The X-ray crystal structure of Li[Zn2(HL1)]4(PO4) 2(PF6)3·(CH3OH) revealed a tetramer of dinuclear complexes, bridged by two phosphate molecules and bifurcating acetic acid arms. Functional studies of the zinc complex with the substrate bis(4-nitrophenyl)phosphate (bNPP) determined the complex with HL12- to be a competent catalyst with kcat = 1.26 ± 0.06 × 10-6 s-1.