Fig. 9: The residue interactions that support peptide binding and access. | Nature Communications

Fig. 9: The residue interactions that support peptide binding and access.

From: Molecular basis of the functional conflict between chloroquine and peptide transport in the Malaria parasite chloroquine resistance transporter PfCRT

Fig. 9

A A Venn diagram of the top 5% of favorable residue interactions for each peptide in the 3D7-PfCRT cavity. B The average potential energy between PfCRT residues and the peptide of interest. Residues for which the potential energy was greater than −10 kJ mol−1, were grouped in ‘other’. The residues are colored by their type, with positively charged residues in blue/purple, negatively charged in red, polar in green, and hydrophobic in light gray.

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