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. Author manuscript; available in PMC: 2020 Dec 30.
Published in final edited form as: Biochemistry. 2020 Jun 12;59(25):2371–2385. doi: 10.1021/acs.biochem.0c00293

Figure 11:

Figure 11:

Potential intramolecular disulfide bond and copper binding site interactions for γS-crystallin. The copper binding sites shown here involve ligands 180° apart with bond distances less than 2.4 Å. (Top left) The bonding interactions are localized to the cysteine loop area of the NTD. (Top right) Potential C23-C83 intramolecular disulfide bond and C25/C27 copper binding site modeled in γS-crystallin using PDBID 6MYG.106 (Bottom right) Alternative possible intramolecular disulfide between C27-C83 and copper binding sites in γS-crystallin modeled using PDBID 2M3T.64 (Bottom left) Copper binding site in S-crystallin between C23 and C27 modeled using PDBID 2M3T.64