Snake venoms are complex mixtures of toxic and often spectacularly biologically active components. Some African vipers contain polyhistidine and polyglycine peptides, which play a crucial role in the interaction with metal ions during the inhibition of snake metalloproteases. Polyhistidine peptide fragments, known as poly-His tags, play many important functions, e.g., in metal ion transport in bacterial chaperon proteins. In this paper, we report a detailed characterization of Cu2+, Ni2+, and Zn2+ complexes with the EDDHHHHHHHHHG peptide fragment (pHG) derived from the venom of the rough scale bush viper (Athens squamigera). In order to determine the thermodynamic properties, stoichiometry, binding sites, and structures of the metal pHG complexes, we used a combination of experimental techniques (potentiometric titrations, electro-spray ionization mass spectrometry, UV-vis spectroscopy, circular dichroism spectroscopy, and electron paramagnetic resonance spectroscopy) and extensive computational tools (molecular dynamics simulations and density functional theory calculations). The results showed that pHG has a high affinity toward metal ions. The numerous histidine residues located along this sequence are efficient metal ion chelators with high affinities toward Cu2+, Ni2+, and Zn2+ ions. The formation of an alpha-helical structure induced by metal ion coordination and the occurrence of polymorphic binding states were observed. It is proposed that metal ions can "move along" the poly-His tag, which serves as a metal ion transport pathway. The coordination of Cu2+, Ni2+, and Zn2+ ions to the histidine tag is very effective in comparison with other histidine-rich peptides. The stabilities of the metal pHG complexes increase in the order Zn2+ < Ni2+ << Cu2+.