Ribbon representation of structural alignment of the N-termini of human LTA4H and lpg2210. (A) The N-terminal domains of human leukotriene A4-hydrolase [PDB:3fun] is shown in cyan and lpg2210 protein from L. pneumophila [PDB:4g2a] is shown in yellow. The alignment has 165 equivalent positions with an RMSD of 3.13 Å, and a P-value of 5.15e-04 determined using FATCAT  with a 5.2% sequence identity. (B) The arrangements of the N- and C-terminal domains in human leukotriene A4 hydrolase [PDB:3fun] is reminiscent of that seen in lpg2210. The central, catalytic domain in the human leukotriene A4 hydrolase (gray in the figure) is missing in lpg2210. The C-terminal, helical domain of LTA4H has a four helical bundle structure, with no statistically significant similarity to the lpg2210 YARHG domain.