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.