Penicillopepsin
From Proteopedia
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| - | {{STRUCTURE_1ppm| PDB=1ppm | SIZE=400| SCENE= |right| CAPTION= | + | {{STRUCTURE_1ppm| PDB=1ppm | SIZE=400| SCENE= |right| CAPTION=Glycosylated penicillopepsin complex with peptide analog and sulfate, [[1ppm]] }} |
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Revision as of 10:28, 15 May 2012
Template:STRUCTURE 1ppm Penicillopepsin (PP) is a proteinase with a broad spectrum of substrates. PP prefers hydrophobic residues at P1 and P1’ sites. PP causes clotting in milk and activates trypsinogen. PP is a member of the aspartic proteinase family. Its extended binding site cleft can bind at least 7 amino acids.
3D structures of penicillopepsin
3app – PjPP – Penicillium janthinellum
1ppl, 1ppm, 1ppk – PjPP + peptide analog
1apt, 1apu, 1apv, 1apw - PjPP + pepstatin analog
2wea, 2web, 2wec, 2wed, 1bxo, 1bxq - PjPP + peptidyl inhibitor
