Introduction: Three-finger toxins (3FTx) are a diverse group of non-enzymatic polypeptides found in snake venoms, known for their broad range of biological activities. This study focuses on a specific 3FTx from the venom of the coral snake Micrurus corallinus (C6JUP0_MICCO). The objective is to identify potential biological targets for this toxin using advanced bioinformatics tools. Methods: The bioinformatics tools employed in this study include AlphaFold2, the DALI server, and Rosetta docking. AlphaFold2 was used to predict the three-dimensional structure of the toxin. The DALI server was then utilized to compare this structure with other known proteins to identify potential structural homologs. Finally, Rosetta docking was applied to predict the toxin's ability to interact with three specific receptors: the nicotinic acetylcholine receptor (nAChR), the muscarinic M1 acetylcholine receptor (M1_mAChR), and the alpha-7 nicotinic acetylcholine receptor (α7_nAChR). Results: The structural analysis using AlphaFold2 revealed that the 3FTx from Micrurus corallinus shares significant similarity with toxins from Hemachatus haemachatus, specifically a cytotoxin homolog (3SOE_HEMHA) and Ringhalexin (3SO1_HEMHA). DALI protein structure comparison confirmed these similarities, suggesting a possible shared functional role. However, the Rosetta docking results indicated that the Micrurus corallinus 3FTx does not establish significant interactions with nAChR, M1_mAChR, or α7_nAChR, which are common targets for many neurotoxic 3FTx. Conclusion: The Micrurus corallinus 3FTx exhibits structural similarities to toxins with known anticoagulant properties rather than neurotoxic effects. This suggests a potential anticoagulant action for this toxin, which aligns with the functional characteristics of its structural homologs from Hemachatus haemachatus. Further experimental studies are required to validate these findings and elucidate the exact biological activities of this 3FTx.