LCN type CS-α/β domain (IPR044062) is a cysteine-stable / (CS-α/β) domain of the LCN type. Interpro database describes that the CS-α/β domain of the LCN type is composed of one or two short -helical segments, and two disulfide bonds are joined to make a triple-stranded -sheet. The variable area is connected to form a loop. Scorpion venoms contain neurotoxins (proteins with a low molecular weight), cardiotoxins, hemolytic toxins, antimicrobial peptides, enzymes (such as hyaluronidase, acetylcholinesterase, phospholipase, and metalloprotease), lipids, nucleotides, and mucopolysaccharides, as well as a complex mixture of biogenic amines. The LCN-type CS-α/β domain is a neurotoxin found in scorpion venom classified as either short-chain or long-chain. They share a structural motif known as the cysteine-stabilized -helix/-sheet motif (CS-α/β). Short LCNs are typically composed of 30-40 residues and three or four disulfide linkages. The majority of short-chain toxins inhibit voltage-dependent or calcium-dependent K + channels. Most long-chain neurotoxins (LCN) include between 60 and 70 residues and are connected by four disulfide links. Long-chain or voltage-gated sodium channel scorpion neurotoxins (NaScTxs) are categorised as alpha toxins (delay the inactivation of Na + channels) or beta toxins (inhibit the inactivation of Na+ channels) (influencing the process of channel activation). Both kinds inhibit inactivation of sodium channels.