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.
CITATION STYLE
Subramanian, E., Liu, M., Swan, I. D., & Davies, D. R. (1977). The crystal structure of an acid protease from Rhizopus chinensis at 2.5 A resolution. Advances in Experimental Medicine and Biology, 95, 33–41. https://doi.org/10.1007/978-1-4757-0719-9_3
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