Variation in structural motifs within SARS-related coronavirus spike proteins
Fig 2
Biliverdin-binding pocket of SARSr-CoV glycoproteins.
The hydrophobic biliverdin binding pocket is formed by the NTD beta sandwich. The corresponding density is rendered as a mesh within the pocket. Residues within 5 Å of biliverdin are displayed. (a) The 007 structure is overlayed with a 1.8 Å reference structure (7B62, tan) known to be bound to biliverdin (lime, molecule from 7B62). Black arrows indicate solvent-exposed carboxyl groups which lack density in the electron maps of all three spikes. (b) The biliverdin density in WIV1 is continuous with the density for some of the pocket residues, namely L110 and N105. (c) The SZ3 map possesses the most isotropic biliverdin density. All SARSr-CoV spikes share conserved Y187 and N105 residues.