Monomeric acetyl-CoA synthase in closed conformation with carbon monoxide bound to the ni proximal of cluster a

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

Ligands and binding sites

• SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A, B
• UWE · $l^{3}-oxidanylidynemethylnickel · ligand · 2 copies · chains A, B
• UW8 · 2-[3,8,8,12,12-pentakis(2-hydroxy-2-oxoethyl)-2,7,11-tris(oxidanylidene)-1,4,6,9,10,13-hexaoxa-5$l^{6}-titanaspiro[4.4^{5}.4^{5}]tridecan-3-yl]ethanoic acid · ligand · chains A, B
• NI · Nickel (II) ion · metal · 2 copies · chains A, B
• CL · Chloride ion · ion · 2 copies · chains A, B
• MLI · Malonate ion · additive · 5 copies · chains B
• PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains B

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

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 767 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

• 7NYS · monomeric acetyl-CoA synthase in closed conformation with carbon monoxide bound to the Ni… · the same entry in another collection · chain A against A, 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 Q3ACS4
• Elsewhere: RCSB PDB 7NYS · PDBe 7NYS · UniProt Q3ACS4