journal menu
![[Figure 1]](ud5057fig1mag.jpg)
|
|
Figure 1
Myricetin-bound crystal structure of SARS-CoV-2 NSP13. (a) Domain organization of NSP13, showing the zinc-binding domain (ZBD; green), stalk domain (wheat), 1B domain (grey), RecA1 domain (orange), RecA2 domain (blue) and the linker connecting the 1B and RecA1 domains (dark grey). Below, a segment of the RecA1 domain and linker highlights the myricetin-interacting amino acids (black). (b) Surface representation of NSP13, colour-coded as in (a), with myricetin displayed as a yellow ball-and-stick model. The positions of the nucleotide-binding site and RNA-binding channel are indicated. The inset shows the binding site with interacting residues (sticks), a water molecule (sphere), hydrogen bonds (red dashed lines), carbon–π interactions (white dashed lines), cation–π interactions (green dashed lines) and donor–π interactions (blue dashed lines). The polder OMIT mFo − DFc electron-density map for myricetin is displayed as a blue mesh, contoured at 4σ. A residual density near the 4′-hydroxyl group is likely to correspond to an alternative water molecule, but it was not included in the model because it fell below the refinement cutoff (map r.m.s.d. < 0.9 e Å−3). The bottom right panel illustrates the chemical structure of myricetin and its interaction network with key NSP13 residues, including hydrogen bonds (red dashed lines), carbon–π interactions (white dashed lines) and cation–π and donor–π interactions (blue–green dashed lines). |
![[Figure 1]](ud5057fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
