Abstract:

A 3D structure of thermostable esterase (EstTs1) was built by means of the protein homology/analogy recognition engine (Phyre) program and further refined via unrestrained dynamics simulation. The docking results reveal that p-nitrophenyl butyrate （C₄） is the best substrate of EstTs1,  which has the adaptive size to the EstTs1. In addition, the key bindingsite residue of Thr111 plays an important role in the catalysis of EstTs1 for it made a hydrogen bond with p-nitrophenyl butyrate. One important finding was that the identification of the key binding site： residue of Ser85 which plays an important role in the catalysis of EstTs1.

Key words: remote homology modeling, docking, thermostable esterase EsTs1