SIRT1 consists of N- and C-domain extensions and a catalytic core [19]. The catalytic domain is formed by the Rossmann fold (components: β1, β2, β6–9, and α1, α7, α8, α12) and the subdomain responsible for zinc binding (α10, α11), the former of which is the dominant subdomain in the catalytic core of Sirtuin 1. The latter, on the other hand, which is smaller, is the result of the fusion of two insertions of the origin of the NAD+ linking domain [20]. The substrate that attaches to the active site, between these subdomains, forces a change in the position of the Rossmann fold and the second domain, resulting in the ability to attach to the sirtuin NAD+. This is defined as a transition of the SIRT1 form from open to closed, and the hydrophobic interdomain groove is then observed to disappear, and the minor subdomain binds to zinc [Zn2+] [21,22]. Various molecules that modulate the activity of the enzyme can bind to the active site. Inauhzin, a SIRT1 inhibitor that was used to limit tumor growth, bound to the active center via hydrophobic bonds and was positioned deep in the interdomain groove between the active site and peripherally attached NAD+ [23]. In the case of EX527, a potent indole inhibitor of SIRT1, it was indicated that interaction with the active site also contributes to changing the conformation of NAD+, sealing the catalytic pocket, and inducing blockade of acetylated lysine access to the substrate in deacetylation reactions [24]. In contrast, resveratrol allosterically modifies the activity of the SIRT1. Resveratrol has shown to bind to the catalytical core of Sirtuin 1 (Figure 1). In the form of three molecules (Res.1, Res.2, and Res.3), it binds in two domains: Res.1 and Res.2 bind to the N-terminal domain (NTD), and Res.3 binds to the C-terminal domain [25]. It is worth noting that at the NTD site, resveratrol molecules also bind to peptides with which SIRT1 cooperates, where they facilitate, for example, bridging between proteins if only in the case of interaction with P53-AMC [26]. Resveratrol activity also facilitates phosphorylation at the C-domain by promoting the binding of SIRT1 to LKB1 (liver kinase B1), one of the components of biogenesis and mitochondrial respiration [27]. Therefore, resveratrol levels may be translated, via SIRT1, into the development of inflammation, regulation of apoptosis, mitochondrial function, and protection from oxidative stress. Among other reasons, sirtuin has become a therapeutic target in reproductive system diseases [28]. Mitochondrial activity, as well as the efficiency of the organization of cell organelles, is one of the keys to achieving good-quality oocytes. Hence, the use of low-dose resveratrol in disease entities involving the ovaries and disorders related to oocyte development appears to be a reasonable approach.