Human SIRT3 in complex with halistanol sulfate

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).

Ligands and binding sites

• 8QF · [(2~{S},3~{S},5~{S},6~{S},8~{S},9~{S},10~{R},13~{R}, 14~{R},17~{R})-17-[(2~{R})-6,6-dimethylheptan-2-yl]-10,13-dimethyl-2,3-disulfooxy-2,3,4,5,6,7,8,9,11,12, 14,15,16,17-tetradecahydro-1~{H}-cyclopenta[a]phenanthren-6-yl] hydrogen sulfate · ligand · 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.

Interfaces

1 interface between chains.

• A–B · 556 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

• 5Y4H · Human SIRT3 in complex with halistanol sulfate · the same entry in another collection · chain A against A, TM-score 1.00
• Q9NTG7 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase sirtuin-3… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9NTG7
• Elsewhere: RCSB PDB 5Y4H · PDBe 5Y4H · UniProt Q9NTG7