Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis

Table 2

Unresolved electron density close to cytosolic cysteine residues in X-ray structures of Na,K-ATPase α-subunit.

PDB ID/Cys position	3WGU	3WGV	3KDP	4HYT	3B8E	S-glutathionylation
204, 242	Density	Density	Small size of density	Small size of density	Small size of density	+
336	Distant density	Distant density	Density	Density	Distant density	+
349	Fragmented density	Fragmented density	nd	nd	nd	+
367, 698	Density	Fragmented density	Distant density	nd	nd	+
421	nd	nd	Small size of density	nd	nd	−
452, 456	Density	Fragmented density	Density	Fragmented density	Density	+
457	Surface	Surface	Surface	Surface	Surface	+
511, 549	Density	Small size of density	nd	nd	nd	+
656	Fragmented density	Fragmented density	nd	nd	nd	+
599	Density	Fragmented density	Density	Density	Density	Not detected
577	Surface	Surface	Surface	Surface	Surface	Not detected

According to MALDI-TOF mass spectrometry data in [13].
“Density”: unresolved density that can fit by glutathione.
“Small size of density”: unresolved density but too small to fit glutathione.
“Distant density”: unresolved electron density at a distance of more than 5  from Cys (glutathione fits density, but the density is far from the residue).
“Fragmented”: no intact unresolved density.
“nd”: no unresolved density close to the residue.