› 5iwg

X-ray diffraction
1.66Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 368 amino acids
Theoretical weight: 42.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92769 (Residues: 8-375; Coverage: 75%)
Gene name: HDAC2
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments

7 bound ligands:
Ligand ZN 3 x ZN
Ligand CA 6 x CA
Ligand IWX 3 x IWX
Ligand PG5 1 x PG5
Ligand PGE 2 x PGE
Ligand PEG 5 x PEG
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 92.297Å b: 98.013Å c: 139.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.208
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The Process and Strategy for Developing Selective Histone Deacetylase 3 Inhibitors.
Cao et al. (2018)
6 more

15 mentions without citation

Non-Hydroxamate Zinc-Binding Groups as Warheads for Histone Deacetylases.
Frühauf et al. (2021)
14 more