Skip to main content
. Author manuscript; available in PMC: 2018 Feb 9.
Published in final edited form as: Chem Rev. 2017 Jul 21;117(15):10474–10501. doi: 10.1021/acs.chemrev.7b00117

Figure 8. Sequence alignment of ARD homologs using ClustalOmega.

Figure 8

The metal binding residues His88, His90, Glu94 and His133 are colored blue, the hydrophobic residues Phe84, Phe105, Phe135 and Ala145 found to be interacting with KMTB are colored red. Arg96 and Arg147 are colored green. Phe149 and Trp155 may be involved in conformational gating are shown in magenta. (All residue numbers refer to the MmARD sequence). The gap in the eukaryotic sequences (corresponding to the sequence APTAETVIAA in Klebsiella is due to a shortened flexible loop D between strand C and helix E (Fig. 3).