Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue‐long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three‐dimensional structural model was obtained in a 50/50% water/2,2,2‐trifluoroethanol‐d3 mixture using two‐dimensional NMR spectroscopy. Maximin 1 was found to adopt an α‐helical structure from residue Ile2 to Ala26. The peptide is amphipathic, showing a clear separation between polar and non‐polar residues. The interactions with sodium dodecyl sulfate micelles, a widely‐used bacterial membrane‐mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an α‐helical conformation, occasionally displaying a flexibility around the Gly9 and Gly16 residues, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with the micelle.