LSD1 also known as AOF2, BHC110, KDM1A a nuclear protein containing a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. LSD1 plays a crucial role in regulating chromatin structure and transcription by removing methyl groups from histone H3, thereby influencing gene expression and maintaining the epigenetic state of the cell. LSD1′s ability to dynamically regulate histone methylation is vital for cellular processes such as differentiation and development, allowing precise control of gene activity in response to various signals. LSD1 contains a SWIRM domain, a flavin adenine dinucleotide (FAD)-binding motif, and an amine oxidase domain, which are essential for enzymatic function. LSD1 interacts with CoREST, a corepressor that enhances demethylation activity and protects against degradation, highlighting the importance of protein-protein interactions in modulating function.