5ER2

High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor. the analysis of the inhibitor binding and description of the rigid body shift in the enzyme

Summary for 5ER2

Entry DOI	10.2210/pdb5er2/pdb
Related PRD ID	PRD_000262
Descriptor	ENDOTHIAPEPSIN, 6-ammonio-N-{[(2R,3R)-3-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1H-imidazol-3-ium-4-yl)-L-alanyl]amino}-4-cyclohexyl-2-hydroxybutyl](2-methylpropyl)carbamoyl}-L-norleucyl-L-phenylalanine (3 entities in total)
Functional Keywords	acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Cryphonectria parasitica (chestnut blight fungus)
Total number of polymer chains	1
Total formula weight	34762.06
Authors	Sali, A.,Veerapandian, B.,Cooper, J.B.,Foundling, S.I.,Hoover, D.J.,Blundell, T.L. (deposition date: 1991-01-02, release date: 1991-04-15, Last modification date: 2017-11-29)
Primary citation	Sali, A.,Veerapandian, B.,Cooper, J.B.,Foundling, S.I.,Hoover, D.J.,Blundell, T.L. High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme. EMBO J., 8:2179-2188, 1989 Cited by PubMed: 2676515 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation