Het-PDB Navi2 (PDB: 1APT)

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Ligands
Code	Name		Style	Show	Link

Non-standard Residues
Code	Name	Show
LTA	4,8-diamino-3-hydroxy-octanoic acid ethyl ester

Glycosylation
Code	Name	Emphasize
MAN	Alpha-D-mannopyranose

Modification
Code	Name	Show
IVA	Isovaleric acid

Download interaction data: 1APT

Code :

1APT 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
1	PENICILLOPEPSIN	E
	ec: 3.4.23.20

mol_id	molecule	chains
2	INHIBITOR ISOVALERYL (IVA)-VAL-VAL-LYSTA-O-ET (LYSTA IS A LYSYL SIDE CHAIN ANALOGUE OF STATIN	I
	other_details: TRANSITION STATE MIMIC INHIBITOR

Source :

mol_id	organism_scientific	organism_common
1	Penicillium janthinellum (taxid:5079)	Penicillium vitale

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

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

PubMed: -1

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

James, M.N.G.,Sielecki, A.R.,Hayakawa, K. et al.
(1992) Biochemistry 31 : 3872

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

Chain :

UniProt :

P00798 (PEPA1_PENJA)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
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
	-	PubMed:4946839

PDB ID: 1APT

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