title: The crystal structure of an acid protease from Rhizopus chinensis at 2.5 A resolution.
abstract: This paper contains a preliminary report of the crystal structure of the acid protease from Rhizopus chinensis at 2.5 A resolution. The molecule is bilobal with a large cleft between the lobes. Pepstatin binds in the cleft near the catalytically active Asp-35. The overall folding of the molecule consists primarily of antiparallel beta-strands, there being only four small helices.
mesh_terms: D001665:Binding Sites; D008958:Models, Molecular; D010436:Pepstatins; D010447:Peptide Hydrolases; D011485:Protein Binding; D011487:Protein Conformation; D012233:Rhizopus / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D010436:Pepstatins; D010447:Peptide Hydrolases