Brand  (β version)

PDB ID: 1PPM

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Ligands
Code Name Style Show Link
0P1 N-[(benzyloxy)carbonyl]-L-alanyl-N-{(1s)-1-[(R)-[(1r)-1-benzyl-2-methoxy-2-oxoethoxy](hydroxy)phosphoryl]-3-methylbutyl }-L-alaninamide PoSSuM
SO4 Sulfate ion PoSSuM
ARA Alpha-L-arabinopyranose PoSSuM
Non-standard Residues
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Glycosylation
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MAN Alpha-D-mannopyranose
Modification
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Structure summary

Code : 1PPM   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/hydrolase inhibitor
Title : CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION-STATE MIMICS BOUND TO PENICILLOPEPSIN: PHOSPHORUS-CONTAINING PEPTIDE ANALOGUES
Release Data : 1993-10-31
Compound :
mol_id molecule chains
1 PENICILLOPEPSIN E
ec: 3.4.23.20
Source :
mol_id organism_scientific
1 Penicillium janthinellum  (taxid:5079)
Authors : Fraser, M.E., James, M.N.G.
Keywords : ACID PROTEINASE, HYDROLASE-hydrolase inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 1.7 Å )
Citation :

Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.

Fraser, M.E.,Strynadka, N.C.,Bartlett, P.A.  et al.
(1992)  Biochemistry  31 : 5201 - 5214

PubMed: 1606144
DOI: 10.1021/bi00137a016

Aspartic Proteinases and Their Catalytic Pathway

James, M.N.G.,Sielecki, A.R.
(1987)  Biological Macromolecules and Assemblies  3 : 413

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

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

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

The Tertiary Structure of Penicillopepsin. Towards a Catalytic Mechanism for Acid Proteases

James, M.N.G.,Hsu, I-N.,Hofmann, T.  et al.
(1981)  STRUCTURAL STUDIES ON MOLECULES OF BIOLOGICA INTERESTL  : 350

An X-Ray Crystallographic Approach to Enzyme Structure and Function

James, M.N.G.
(1980)  Can.J.Biochem.  58 : 251

Structural Evidence for Gene Duplication in the Evolution of the Acid Proteases

Tang, J.,James, M.N.G.,Hsu, I.N.  et al.
(1978)  Nature  271 : 618

Mechanism of Acid Protease Catalysis Based on the Crystal Structure of Penicillopepsin

James, M.N.G.,Hsu, I.-N.,Delbaere, L.T.J.
(1977)  Nature  267 : 808

Penicillopepsin from Penicillium Janthinellum Crystal Structure at 2.8 Angstroms and Sequence Homology with Porcine Pepsin

Hsu, I.-N.,Delbaere, L.T.J.,James, M.N.G.  et al.
(1977)  Nature  266 : 140

Penicillopepsin. 2.8 Angstroms Structure, Active Site Conformation and Mechanistic Implications

Hsu, I-N.,Delbaere, L.T.J.,James, M.N.G.  et al.
(1977)  Adv.Exp.Med.Biol.  95 : 61

The Crystal Structure of Penicillopepsin at 6 Angstroms Resolution

Hsu, I-N.,Hofmann, T.,Nyburg, S.C.  et al.
(1976)  Biochem.Biophys.Res.Commun.  72 : 363

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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