Het-PDB Navi2 (PDB: 1EPR)

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Ligands
Code	Name		Style	Show	Link
0QS	N~2~-[(2r)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1r)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1h-imidazol-3-ium-4-yl)-L-alaninamide				PoSSuM

Non-standard Residues
Code	Name	Show
DGN	D-glutamine

Glycosylation
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Modification
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Download interaction data: 1EPR

Code :

1EPR PDBj RCSB PDB PDBe

Header :

HYDROLASE/HYDROLASE INHIBITOR

Title :

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-135,040

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 :

Badasso, M., Crawford, M., Cooper, J.B., Blundell, T.L.

Keywords :

HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ACID PROTEINASE

Exp. method :

X-RAY DIFFRACTION ( 2.3 Å )

Citation :

A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.

Bailey, D.,Cooper, J.B.
(1994) Protein Sci. 3 : 2129 - 2143

PubMed: 7703859

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: 1EPR