Fig. 6: Chromophore binding of SasPcob and BV docking into AbPcob.

AdoCbl (a) and and BV (b) binding in SasPcob. Protein residues are shown as orange sticks. Residues from the other protein chain are shown as blue sticks. AdoCbl and BV molecules are shown as yelllow and pink sticks, respectively, and water molecules as blue spheres. Structurally-relevant water molecules are shown as green spheres. Salt-bridges and their centres are shown as yellow dashes and cyan spheres, hydrophobic interactions as a blue dash and hydrogen bonds as a red dash. c–f Clustered AbPcob protein structures after MD simulations, showing possible binding pose with BV. The grey cartoon and sticks are the representations for SasPcob as comparision. BV molecule and its binding region in AbPcob are coloured as yellow sticks and red cartoon. Residues involved with BV binding are shown as red sticks. The blue dashes indicate hydrophobic interactions between BV and AbPcob protein residues. Comparison of BV binding in AbPcob (g, modelled) and SasPcob (h, crystal structure). Binding poses in cluster 6 were selected for comparison (see Supplementary Table 1 for clusters summary). BV and B12 molecules are shown as above. Residues around BV with 4 Å are shown as red (AbPcob) and grey (SasPcob) sticks.