1ENT

X-RAY ANALYSES OF ASPARTIC PROTEINASES. THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN

Summary for 1ENT

Entry DOI	10.2210/pdb1ent/pdb
Related PRD ID	PRD_000264
Descriptor	ENDOTHIAPEPSIN, 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, SULFATE ION, ... (4 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	34669.75
Authors	Blundell, T.L.,Dealwis, C.G. (deposition date: 1992-03-11, release date: 1994-01-31, Last modification date: 2017-11-29)
Primary citation	Blundell, T.L.,Jenkins, J.A.,Sewell, B.T.,Pearl, L.H.,Cooper, J.B.,Tickle, I.J.,Veerapandian, B.,Wood, S.P. X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin. J.Mol.Biol., 211:919-941, 1990 Cited by PubMed: 2179568 DOI: 10.1016/0022-2836(90)90084-Y PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation