In order to investigate the role of superoxide dismutase (SOD) gene family members in the self-incompatibility response of Camellia oleifera, three family members CoCSD, CoFSD and CoMSD were isolated by RT-PCR. The CDS sequences of CoCSD, CoFSD and CoMSD were 660, 813 and 693 bp in length, encoding for 219, 270 and 230 amino acids, with a molecular weight of 22.49 kDa, 31.18 kDa and 25.51 kDa, respectively. Structural analysis revealed that three proteins were hydrophilic without transmembrane domain and signal peptide (non-secretory proteins), and all contained 21 phosphorylation sites. Both CoCSD and CoMSD are stable, while CoFSD is an unstable protein. The secondary structure of CoCSD is mainly composed of irregularly coiled and extended chains, while the secondary structure of CoFSD and CoMSD is mainly composed of α-helices and irregular coils. The three proteins were assigned to three categories in the phylogenetic tree, whereas all were clustered on the same branchlet with the corresponding proteins of tea tree and had high sequence homology. The SOD enzyme activity in self-pollinated pistils was overall higher than that in cross-pollinated pistils, but the expression of CoCSD, CoFSD and CoMSD was highest before pollination and was inhibited by both self and cross-pollination treatments. The results of this study lay the foundation for the subsequent in-depth investigation of the biological functions of C. oleifera SOD genes, and also provide a reference for revealing the mechanism of self-incompatibility in C. oleifera.