› 4lxz

X-ray diffraction
1.85Å 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: 369 amino acids
Theoretical weight: 42.37 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q92769 (Residues: 8-376; Coverage: 76%)
Gene name: HDAC2
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments

6 bound ligands:
Ligand ZN 3 x ZN
Ligand CA 3 x CA
Ligand NA 3 x NA
Ligand PG4 8 x PG4
Ligand SHH 3 x SHH
Ligand NHE 1 x NHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 91.967Å b: 97.603Å c: 138.833Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.192
Expression system: Spodoptera frugiperda

Quick links

Citations

26 review citations

Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents.
Mottamal et al. (2015)
25 more

66 mentions without citation

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
65 more