HST2 bound to ADP-hpd, acetyllated histone H4 and nicotinamide

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).

Ligands and binding sites

• A1R · 5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-dihydroxypyrrolidin-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy) phosphoryl]adenosine · ligand · chains A, B
• NCA · Nicotinamide · 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 · 622 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

• 2QQG · Hst2 bound to ADP-HPD, acetyllated histone H4 and nicotinamide · 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 0.93
• P02309 · AlphaFold monomer V2.0 prediction for histone H4 (P02309) · a predicted model of the same protein · chain B against A, TM-score 0.32

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 2QQG · PDBe 2QQG · UniProt P53686 · UniProt P02309