Abstract
The structure of subtilisin BPN' at a resolution of 2.5 Å reveals an interesting active-site hydrogen-bond network involving the side chains of Asp 32, Ser 33, His 64, and reactive Ser 221. This network becomes of even greater interest when it is compared with the corresponding region in another serine protease, α-chymotrypsin. Although the two enzymes have entirely different three-dimensional structures, their active-site regions are remarkably similar.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Structure-Function Relationships of Proteolytic Enzymes
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
