The above domain search and protein docking results show that the N-terminal BPI1/LBP domain of extracellular ORF7a has functioned as binding lipopolysaccharide, the C-terminal and middle part of extracellular ORF7a bind CD14. Therefore, we believed extracellular ORF7a had similar LBP activity and could help to form the LPS-ORF7a-CD14 complex, then ORF7a fell off and promoted the binding of LPS and CD14. However, the N-terminal of extracellular ORF7a is outside the N-terminal active pocket of CD14. We speculated that the two ATP-supplying energy structures promoted the rotation of the extracellular ORF7a around the two ATP sites' central axis and accurately delivered the N-terminal LPS into the N-terminal active pocket of CD14.