Antifreezing proteins (AFPs) have been found in many organisms ranging from bacteria to vertebrates that inhabit subzero environments. AFPs are believed to adsorb the surface of nascent ice crystals and prevent water molecules from accessing the ice surface at the bound location. We here focused on AFP from Rhagium inquisitor (RiAFP) as a target and performed molecular dynamics (MD) simulations of RiAFP on ice surface in water below melting temperature to investigate how RiAFP affects the ice growth. It was found that the ice growth from the prismatic face is suppressed and that from the basal face is accelerated, respectively due to the RiAFP binding. Furthermore, mutations to RiAFP, where all Thr are replaced by Gly, resulted in loss of antifreezing nature due to reduced binding to the ice surface.