The C-ring ion binding site of the ATP synthase from bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

Structure

x-ray diffraction · 1 distinct chain · 96% helix, 0% strand (DSSP).

Ligands and binding sites

• DPV · dodecyl 2-(trimethylammonio)ethyl phosphate · ligand · 13 copies · chains A, B, M, C, D, E, F, G, H, I, J, K, L
• NA · Sodium ion · metal · 10 copies · chains B, C, D, E, F, G, H, I, J, K, L, M
• LMT · Dodecyl-beta-D-maltoside · additive · chains A, B, C

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

13 interfaces between chains.

• K–L · 1491 Ų buried · 1 hydrogen bond · protein-protein
• A–M · 1472 Ų buried · 3 hydrogen bonds · protein-protein
• H–I · 1440 Ų buried · 1 hydrogen bond · protein-protein
• A–B · 1439 Ų buried · 1 hydrogen bond · protein-protein
• D–E · 1437 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 13 modified (formylation).

Compared structures

• 4CBK · The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted… · the same entry in another collection · chain K against K, TM-score 1.00

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 P22483
• Elsewhere: RCSB PDB 4CBK · PDBe 4CBK · UniProt P22483