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The CG portion of GSH anchors the two adjacent protomers via not only these salt bridges, but also by additional H-bonding interactions with Y231 of protomer A and the carbonyl oxygen of W154 of protomer B via a bridging water molecule

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This is exemplified by bottom-up MS analysis of the covalent adduct of SUMO-activating enzyme (SUMO E1 or SAE) with inhibitor COH000 [70] (Figure 4B): pepsin-mediated proteolytic peptide A14–L32 was found in the untreated sample, but the covalent modification of Cys30 in the COH000-treated sample blocked access to the pepsin cleavage site after Leu32, resulting in the simple COH000 adduct of peptide A14–N35 (missed cleavage)