Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin

The polypeptide chain of the acid protease penicillopepsin folds via an 18-stranded mixed β-sheet into two distinct lobes separated by a 30-Å long groove which is the extended substrate binding site. The catalytic residues Asp-32 and Asp-215 are located in this groove and their carboxyl groups are in intimate contact. Alignment of the amino acid sequence with that of pepsin shows regions of high homology.

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