ATP synthase C10 ring reacted with dccd at pH 5.5

Structure

x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).

Ligands and binding sites

• DCW · Dicyclohexylurea · ligand · 5 copies · chains K, L, M, N, O

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

4 interfaces between chains.

• L–M · 1519 Ų buried · 3 hydrogen bonds · protein-protein
• N–O · 1514 Ų buried · 4 hydrogen bonds · protein-protein
• K–L · 1509 Ų buried · 3 hydrogen bonds · protein-protein
• M–N · 1506 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 covalent, 5 modified (covalent ligand, formylation).

Compared structures

• 3U32 · ATP synthase c10 ring reacted with DCCD at pH 5.5 · the same entry in another collection · chain O against O, TM-score 1.00
• P61829 · AlphaFold monomer V2.0 prediction for ATP synthase subunit 9, mitochondrial (P61829) · a predicted model of the same protein · chain M against A, TM-score 0.97

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 P61829
• Elsewhere: RCSB PDB 3U32 · PDBe 3U32 · UniProt P61829