Structure and mechanism of acetylation by the N-terminal dual enzyme NATA/NAA50 complex

Structure

x-ray diffraction · 3 distinct chains.

Ligands and binding sites

• ACO · Acetyl coenzyme *A · ligand · chains C
• IHP · Inositol hexakisphosphate · ligand · chains A, B
• CL · Chloride ion · ion · 18 copies · chains C, A, B
• GOL · Glycerol · additive · 8 copies · chains C, A, B
• MLI · Malonate ion · additive · 4 copies · chains A, B
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B

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

Compared structures

• 6O07 · Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex · the same entry in another collection · chain C against C, TM-score 1.00
• Q08689 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase NAT5 (Q08689) · a predicted model of the same protein · chain C against A, TM-score 0.96
• P07347 · AlphaFold monomer V2.0 prediction for N-terminal acetyltransferase a complex catalytic… · a predicted model of the same protein · chain B against A, TM-score 0.89

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 Q08689
• Every structure of UniProt G2WCC0
• Every structure of UniProt P07347
• Elsewhere: RCSB PDB 6O07 · PDBe 6O07 · UniProt Q08689 · UniProt G2WCC0 · UniProt P07347