In the present study, we used GRAMPA, the giant repository of AMPs, counting 6,760 unique sequences . Despite the abundance of sequences, the structural information of most AMPs remains unclear as only a tiny fraction (2.5%) have a resolved structure . Not many databases provide information on the number of structures they contain, but in the case of APD , the majority (60.41%) of its sequences have no known structure, 15.20% are peptides with identified disulfide bonds but lack a tridimensional structure, while 14.38% are α-helical peptides, and just 2.59% have βsheet structures. This distribution is likely similar across other databases, indicating a significant gap in our understanding of AMP structures and the greater prevalence of α-helices. Here, we benchmarked four protein structure prediction methods -Jpred4 46 , PEP2D , PSIPRED 48 , AlphaFold2 49 -using 261 curated and experimentally known structures from the PDBe database. We applied our best structure predictor to map the structural landscape of GRAMPA, the giant yet vastly uncharted repository of antimicrobial peptides.