Het-PDB Navi2 (PDB: 1EPQ)

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Ligands
Code	Name		Style	Show	Link
0QF	N-[(1s)-2-{[(2s,3r,4s)-1-cyclohexyl-3,4-dihydroxy-6-methylheptan-2-yl]amino}-1-(ethylsulfanyl)-2-oxoethyl]-nalpha-(morpholin-4-ylsulfonyl)-L-phenylalaninamide				PoSSuM
SO4	Sulfate ion				PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 1EPQ

Code :

1EPQ PDBj RCSB PDB PDBe

Header :

HYDROLASE/HYDROLASE INHIBITOR

Title :

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-133,450 (SOT PHE GLY+SCC GCL)

Release Data :

1994-12-20

Compound :

mol_id	molecule	chains
1	ENDOTHIAPEPSIN	E
	ec: 3.4.23.22

Source :

mol_id	organism_scientific	organism_common
1	Cryphonectria parasitica (taxid:5116)	Chestnut blight fungus

Authors :

Dealwis, C., Cooper, J.B., Blundell, T.L.

Keywords :

HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ACID PROTEINASE

Exp. method :

X-RAY DIFFRACTION ( 1.9 Å )

Citation :

Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.

Lunney, E.A.,Hamilton, H.W.,Hodges, J.C. et al.
(1993) J.Med.Chem. 36 : 3809 - 3820

A Structural Comparison of 21 Inhibitor Complexes of the Aspartic Proteinase from Endothia Parasitica

Bailey, D.,Cooper, J.B.
To be Published

The 3D Structure at 2 Angstroms Resolution of Endothiapepsin

Blundell, T.L.,Jenkins, J.,Sewell, B.T. et al.
(1990) J.Mol.Biol. 211 : 919

Chain :

UniProt :

P11838 (CARP_CRYPA)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-\|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.	3.4.23.22	-
	-	-

PDB ID: 1EPQ