Structural basis of a novel proton-coordination type in an F1FO-ATP synthase rotor ring

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

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 · 1489 Ų buried · 2 hydrogen bonds · protein-protein
• C–D · 1454 Ų buried · 2 hydrogen bonds · protein-protein
• A–B · 1436 Ų buried · 1 hydrogen bond · protein-protein
• F–G · 1435 Ų buried · 0 hydrogen bonds · protein-protein
• E–F · 1431 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 modified (formylation).

Compared structures

• 2X2V · Structural basis of a novel proton-coordination type in an F1Fo-ATP synthase rotor ring · 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 2X2V · PDBe 2X2V · UniProt P22483