Structures of chloramphenicol acetyltransferase III and Escherichia coli β-ketoacylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(dethia)CoA

Benjamin, A.B.; Stunkard, L.M.; Ling, J.; Nice, J.N.; Lohman, J.R.

doi:10.1107/S2053230X23001206

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 3
Active-site interactions of AcOCoA with CATIII and chloramphenicol co-substrate. Note that a water bound to chloramphenicol helps to create the oxyanion hole, which is circled in red.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 79| Part 3| March 2023| Pages 61-69

https://doi.org/10.1107/S2053230X23001206

Open

access

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page