The three-dimensional X-ray crystal structure of the aspartic proteinase native to Trichoderma reesei complexed with a renin inhibitor CP-80794.
Pitts
J E
JE
Department of Crystallography, Birkbeck College, University of London, United Kingdom.
Crawford
M D
MD
Nugent
P G
PG
Wester
R T
RT
Cooper
J B
JB
Mantyla
A
A
Fagerstrom
R
R
Nevalainen
H
H
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009025:Morpholines / Q000737:chemistry / Q000378:metabolism*; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology*; D000092502:Renin Inhibitors
D016282:Aspartic Acid Endopeptidases; D004151:Dipeptides; D009025:Morpholines; D011480:Protease Inhibitors; D000092502:Renin Inhibitors; C076964:terlakiren