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Ligands
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0EO (2s)-2-[[(3s,4s)-5-cyclohexyl-4-[[(4s,5s)-5-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxidanyl-6-phenyl-hexanoyl]amino]-3-oxidanyl-pentanoyl]amino]-4-methyl-pentanoic acid
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Code : 1EED   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors
Release Data : 1994-01-31
Compound :
mol_id molecule chains
1 ENDOTHIAPEPSIN P
ec: 3.4.23.22
Source :
mol_id organism_scientific organism_common
1 Cryphonectria parasitica  (taxid:5116) Chestnut blight fungus
Authors : Blundell, T.L., Frazao, C., Cooper, J.B.
Keywords : ASPARTIC PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.

Cooper, J.,Quail, W.,Frazao, C.  et al.
(1992)  Biochemistry  31 : 8142 - 8150

PubMed: 1525155
DOI: 10.1021/bi00150a005

Chain : P
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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