journal menu
![[Figure 1]](xh5065fig1mag.jpg)
|
|
Figure 1
Representative structure of NcAA9D (PDB entry 9z8o). (a) The two chains of NcAA9D (chain A in purple and chain B in green) are arranged carbohydrate-binding face to carbohydrate-binding face, secluding the active sites from the bulk solvent and facilitating the formation of two pre-bound dioxygen sites. (b) The active and pre-bound dioxygen sites of chain A in NcAA9D. In the Cu(II) state, the active-site copper is coordinated by the histidine brace and an axial and equatorial water. In NcAA9D, a pre-bound dioxygen species is observable just past the equatorial water. It is surrounded by His157, Gln166, and Glu30 from the opposing chain. All visualizations of the protein structure and electron-density maps were created in ChimeraX (v1.8; Meng et al., 2023  ). |
![[Figure 1]](xh5065fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
