Docking results showing binding sites of VHHs on surfaces of PLA₂s.

<p>(A) KF498607 (blue ribbon) and BthTX-I (red surface); (B) KC329718 (blue ribbon) and BthTX-I (red surface); (C) KF498607 (blue ribbon) and BthTX-II (orange surface); (D) KC329718 (blue ribbon) and BthTX-II (orange surface). The interaction sites were enlarged to show hydrogen bonds formed between the amino acid residues. Both VHHs covered the enzymatic groove surface areas of the modeled BthTX-II and inserted the CDR3 into the catalytic cleft, as well as being able to interact with amino acid residues of the PLA₂ C-termini.