Structure of the yeast HST2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 18% strand (DSSP).

Ligands and binding sites

• OAD · 2'-O-acetyl adenosine-5-diphosphoribose · ligand · chains A, B
• ZN · Zinc ion · metal · chains A

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 693 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

• 1Q1A · Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP… · the same entry in another collection · chain A against A, TM-score 1.00
• P53686 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase HST2 (P53686) · a predicted model of the same protein · chain A against A, TM-score 0.99
• P02309 · AlphaFold monomer V2.0 prediction for histone H4 (P02309) · a predicted model of the same protein · chain B against A, TM-score 0.25

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 P53686
• Every structure of UniProt P02309
• Elsewhere: RCSB PDB 1Q1A · PDBe 1Q1A · UniProt P53686 · UniProt P02309