Acta Crystallographica Section D
Acta Crystallographica
Section D
STRUCTURAL BIOLOGY
IUCr
IT
WDC
search IUCr Journals
home
archive
editors
for authors
for readers
submit
subscribe
open access
journal menu
home
archive
editors
for authors
for readers
submit
subscribe
open access
research papers
Share
Share
Issue contents
Article statistics
Download citation
Format
BIBTeX
EndNote
RefMan
Refer
Medline
CIF
SGML
Text
Plain Text
Download PDF of article
Acta Cryst.
(2014).
D
70
,
607-614
https://doi.org/10.1107/S1399004713031222
Download PDF of article
Download citation
Format
BIBTeX
EndNote
RefMan
Refer
Medline
CIF
SGML
Text
Plain Text
Article statistics
Issue contents
Share
Open
access
Structure of
Bacillus subtilis
γ-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue
T. Ida
,
H. Suzuki
,
K. Fukuyama
,
J. Hiratake
and
K. Wada
The binding modes of acivicin, a classical and an electrophilic active-site-directed glutamate analogue, to bacterial γ-glutamyltranspeptidases were found to be diverse.
Keywords:
γ-glutamyltranspeptidase
;
inhibitors
;
acivicin
;
glutamine antagonist
;
glutathione
;
glutamine amidotransferase
;
Ntn-hydrolase family
.
Read article
Similar articles
Follow Acta Cryst. D
E-alerts
Twitter
Facebook
RSS