Rb+-bound E2-MgF state of the gastric proton pump (Wild-type)

Structure

x-ray diffraction · resolution 4.3 · 3 distinct chains · 35% helix, 16% strand (DSSP).

Ligands and binding sites

• MF4 · Tetrafluoromagnesate(2-) · ligand · 2 copies · chains A, E
• CLR · Cholesterol · ligand · 2 copies · chains A, B, F, E
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains B, F
• K · Potassium ion · metal · 6 copies · chains A, E
• MG · Magnesium ion · metal · 2 copies · chains A, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• F–E · 2246 Ų buried · 34 hydrogen bonds · protein-protein
• A–B · 2220 Ų buried · 28 hydrogen bonds · protein-protein
• A–E · 228 Ų buried · 0 hydrogen bonds · protein-protein
• A–F · 177 Ų buried · 3 hydrogen bonds · protein-protein
• B–E · 128 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 glycan, 6 disulfide (N-glycosylation, disulfide).

Compared structures

• 6JXK · Rb+-bound E2-mgf state of the gastric proton pump (wild-type) · the same entry in another collection · chain F against F, TM-score 1.00
• P19156 · AlphaFold monomer V2.0 prediction for potassium-transporting ATPase alpha chain 1 (P19156) · a predicted model of the same protein · chain A against A, TM-score 0.99
• P18434 · AlphaFold monomer V2.0 prediction for potassium-transporting ATPase subunit beta (P18434) · a predicted model of the same protein · chain F against A, TM-score 0.94

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P19156
• Every structure of UniProt P18434
• Elsewhere: RCSB PDB 6JXK · PDBe 6JXK · UniProt P19156 · UniProt P18434