Crystal structure of myst acetyltransferase domain in complex with acetyl-CoA cofactor

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Ligands and binding sites

• ACO · Acetyl coenzyme *A · ligand · chains A
• 7L1 · S-{(3S,5R,9R)-1-[(2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]-3, 5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2, 4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} ethanethioate · ligand · chains A
• NA · Sodium ion · metal · 3 copies · chains A
• ZN · Zinc ion · metal · chains A

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

Pockets

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

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

• 6BA4 · Crystal structure of MYST acetyltransferase domain in complex with Acetyl-CoA cofactor · the same entry in another collection · chain A against A, TM-score 1.00
• Q9H7Z6 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9H7Z6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9H7Z6
• Elsewhere: RCSB PDB 6BA4 · PDBe 6BA4 · UniProt Q9H7Z6