It started off as a Cys, how did it end up like this? Identifying the extent of unmodelled oxidatively modified cysteines within the Protein Data Bank

Foster, S.P.; Warren, A.J.; Siebert, C.A.; Basran, J.; Moody, P.C.E.

doi:10.1107/S2059798326003943

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 9
Preferential oxidation of active-site cysteines in GAPDHs. The active-site cysteine in hpGAPDHA (Cys149, red) is oxidized in the NADP holoenzyme structure, whereas the three other cysteines within the subunit (Cys16, Cys96 and Cys262, yellow) are not. The locations of the Pi site and NADP are also shown. This figure was created from PDB entry 9fq4 (Foster, 2025

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 82| Part 7| July 2026|

https://doi.org/10.1107/S2059798326003943

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