Abstract: The characterization of proteins from thermophilic organisms is becoming more and more interesting for possible biotechnological applications. Recently, the complete genome of a hyper-thermophilic archaebacterium, P. horikoshii, was sequenced [1] and a sugar binding protein (Ph-SBP) was identified by means of analysis of its sequence similarity. Some preliminary experimental information are available on its binding properties and on its structural features; however, the lack of information about its 3D structure impairs the complete knowledge of its conformational properties and interactions with its ligands. Here, we present the results of the homology modelling strategy we used to predict the 3D structure of Ph-SBP, and the analysis we made on the resulting model in order to assess its reliability, with particular care to its expected thermostability features and sugar binding properties.