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Function
The ASP protein is a serine protease of the subtilisin family and it will cut peptide bonds after specific amino acids.
Structure
The ASP protein contains an N-terminal region that forms the subtilisin domain and a C-terminal region that forms the P-domain.
The subtilisin domain is composed of ten helices and twelve chains. The structure of the P-domain is a jelly roll-like fold with eight beta-strands.
The structure contains calcium ions.
The catalytic triad of ASP is composed of Asp78, His115 and Ser336.
Disease
Relevance
Structural highlights
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