Brand  (β version)

PDB ID: 1ENT

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Ligands
Code Name Style Show Link
0EM N-(tert-butoxycarbonyl)-L-phenylalanyl-N-{(1s)-1-[(R)-hydroxy(2-{[(2s)-2-methylbutyl]amino}-2-oxoethyl)phosphoryl]-3-methylbutyl}-3-(1h-imidazol-3-ium-4-yl)-L-alaninamide PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1ENT   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : X-RAY ANALYSES OF ASPARTIC PROTEINASES. THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN
Release Data : 1994-01-31
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 : Blundell, T.L., Dealwis, C.G.
Keywords : ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.9 Å )
Citation :

X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.

Blundell, T.L.,Jenkins, J.A.,Sewell, B.T.  et al.
(1990)  J.Mol.Biol.  211 : 919 - 941

PubMed: 2179568
DOI: 10.1016/0022-2836(90)90084-Y

X-Ray Analyses of Aspartic Proteinases. III Three-Dimensional Structure of Endothiapepsin Complexed with a Transition-State Isostere Inhibitor of Renin at 1.6 Angstroms Resolution

Veerapandian, B.,Cooper, J.B.,Sali, A.  et al.
(1990)  J.Mol.Biol.  216 : 1017

Reaction

Chain : E
UniProt : P11838 (CARP_CRYPA)
Reaction: EC: Evidence:
Physiological Direction:
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 -
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