Brand  (β version)

PDB ID: 1APU

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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
32L Ethyl (3s,4s)-4-amino-3-hydroxy-6-methylheptanoate
Glycosylation
Code Name Emphasize
MAN Alpha-D-mannopyranose
Modification
Code Name Show
IVA Isovaleric acid

Structure summary

Code : 1APU   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystallographic analysis of a pepstatin analogue binding to the aspartyl proteinase penicillopepsin at 1.8 angstroms resolution
Release Data : 1994-01-31
Compound :
mol_id molecule chains synonym
1 PROTEIN (PENICILLOPEPSIN) E Peptidase A
ec: 3.4.23.20
mol_id molecule chains
2 PEPSTATIN ANALOGUE ISOVALERYL-VAL-VAL-STA-O-ET I
Source :
mol_id organism_scientific
1 Penicillium janthinellum  (taxid:5079)
mol_id organism_scientific
2
Authors : Sielecki, A.R., James, M.N.G.
Keywords : ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 1.8 Å )
Citation :

Crystallographic Analysis of Transition State Mimics Bound to Penicillopepsin: Difluorostatine-and Difluorostatone-Containing Peptides

James, M.N.G.,Sielecki, A.R.,Moult, J.
(1992)  Biochemistry  31 : 3872

Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution

James, M.N.G.,Sielecki, A.R.,Hayakawa, K.  et al.
(1983)  Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium  1 : 521

PubMed: -1

Aspartic Proteinases and Their Catalytic Pathway

James, M.N.G.,Sielecki, A.R.
(1987)  Biological Macromolecules and Assemblies  3 : 414

Stereochemical Analysis of Peptide Bond Hydrolysis Catalyzed by the Aspartic Proteinase Penicillopepsin

James, M.N.G.,Sielecki, A.R.
(1985)  Biochemistry  24 : 3701

X-Ray Diffraction Studies on Penicillopepsin and its Complexes: The Hydrolytic Mechanism

James, M.N.G.,Sielecki, A.R.,Hofmann, T.
(1985)  Aspartic Proteinases and Their Inhibitors  : 163

Effect of Ph on the Activities of Penicillopepsin and Rhizopus Pepsin and a Proposal for the Productive Substrate Binding Mode in Penicillopepsin

Hofmann, T.,Hodges, R.S.,James, M.N.G.
(1984)  Biochemistry  23 : 635

Structure and Refinement of Penicillopepsin at 1.8 Angstroms Resolution

James, M.N.G.,Sielecki, A.R.
(1983)  J.Mol.Biol.  163 : 299

Conformational Flexibility in the Active Sites of Aspartyl Proteinases Revealed by a Pepstatin Fragment Binding to Penicillopepsin

James, M.N.G.,Sielecki, A.,Salituro, F.  et al.
(1982)  Proc.Natl.Acad.Sci.USA  79 : 6137

Reaction

Chain : E
UniProt : P00798 (PEPA1_PENJA)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen. 3.4.23.20 PubMed:4946839
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