Literature DB >> 596305

The crystal structure of an acid protease from Rhizopus chinensis at 2.5 A resolution.

E Subramanian, M Liu, I D Swan, D R Davies.   

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.

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Year:  1977        PMID： 596305     DOI： 10.1007/978-1-4757-0719-9_3

Source DB:  PubMed          Journal:  Adv Exp Med Biol        ISSN： 0065-2598            Impact factor:   2.622


  1 in total

1.  Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.

Authors:  K Suguna; E A Padlan; C W Smith; W D Carlson; D R Davies
Journal:  Proc Natl Acad Sci U S A       Date:  1987-10       Impact factor: 11.205
  1 in total

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