Literature summary for 3.4.23.22 extracted from

Coates, L.; Erskine, P.T.; Wood, S.P.; Myles, D.A.; Cooper, J.B.
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism (2001), Biochemistry, 40, 13149-13157.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure studied by neutron crystallography, crystals are monocliic, P2(1), unit cell dimensions a : 43.1 A, b : 75.7 A, c : 42.9 A, endothiapepsin-H261 complex	Endothia sp.

Inhibitors	Comment	Organism	Structure
H261	-	Endothia sp.

Organism	UniProt	Comment	Textmining
Endothia sp.	-	-	-

Synonyms	Comment	Organism
Aspartic proteinase	-	Endothia sp.

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)