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PDBe Entry: 1apt 
CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO THE ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION
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HYDROLASE(ACID PROTEINASE)
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X-RAY DIFFRACTION
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Resolution: 1.8 Å, R-factor: 13.5%, Spacegroup: C 1 2 1
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31/01/1994, deposition: 16/12/1991, last revision: 25/08/2009
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Sielecki, A.R.; James, M.N.G.
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Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution
Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium vol:1, pag:521 (1983) Pierce Chemical Company,Rockford,Il
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HYDROLASE(ACID PROTEINASE)
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3.4.23.20 ExPASy BRENDA (E)
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Penicillium janthinellum 5079(E)
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Penicillopepsin (EC 3.4.23.20) (Peptidase A) P00798 (E)
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E, I
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| E |
PENICILLOPEPSIN |
Protein |
P00798 (PENP_PENJA)
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323 |
100% |
| I |
INHIBITOR ISOVALERYL (IVA)-VAL-VAL-LYSTA-O-ET (LYSTA IS A LYSYL SIDE CHAIN ANALOGUE OF STATIN |
Protein |
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4 |
100% |
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| E |
SUGAR (ALPHA-D-MANNOSE) |
MAN
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