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In all three structures, an additionally bound N-morpholino-ethansulfonic acid molecule from the buffer solution was found

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This enables Cagri to form conserved interactions when bound to CTR and AMYRs, including the inter-peptide contacts that facilitate the formation and stabilisation of the bypass motif and the intramolecular salt bridge (E14 Cagri and R17 Cagri )

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The copper chelation capacity of AHK-Cu distinguishes it from unchelated peptide analogs, enabling research into coppers role as a cofactor in angiogenic and wound-response signaling