Yeasts of the genus Candida have been considered of great biotechnological value for more than 30 years. Candida tropicalis has gained much interest due to its ability to synthesize xylitol, a pentahydroxy sugar alcohol intermediate of xylose catabolism, which is used in the food and confectionery industry as a natural sweetener. In the present work, the xylitol dehydrogenase (XYL2) from C. tropicalis was investigated in order to achieve its structural classification. Analyses of this protein sequence were performed by bioinformatics tools and the structural model of this protein was obtained by homology modeling. The homologous proteins were found from an sequence alignment against the protein data bank (PDB) using Blastp. The structural model for XYL2 was obtained using the EsyPred-3D server, and the structural neighbors search was performed with the Vector Alignment Search Tool (VAST). The energy refinement of the XYL2/NAD⁺/zinc complex model was done using molecular mechanics tools available on SPDBV with Gromos96 package. The selected three-dimensional structures of alcohol dehydrogenases from PDB were superimposed to XYL2 considering the NAD⁺ and zinc binding domains using MultiProt server and the CCP4 program package, and the r.m.s.d. family of overall was generated. The analysis of XYL2 sequence, indicated that the enzyme presents the zinc-containing alcohol dehydrogenases signatures [GHE]xx[G]xxxxx[G]xx[V], the active site for only one zinc ion and the active site for NAD⁺ binding. Based on all these results we propose that XYL2 is a NAD⁺/zinc-binding protein and belongs to the MDR (medium-chain-dehydrogenase/reductase) superfamily.