› 7zzp

X-ray diffraction
1.52Å 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:
Cellular component:
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: 498 amino acids
Theoretical weight: 56.56 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q92769 (Residues: 1-488; Coverage: 100%)
Gene name: HDAC2
Sequence domains: Histone deacetylase domain

Ligands and Environments

11 bound ligands:
Ligand ZN 3 x ZN
Ligand CA 3 x CA
Ligand NA 3 x NA
Ligand PGE 4 x PGE
Ligand EDO 9 x EDO
Ligand KJ6 4 x KJ6
Ligand 2OP 3 x 2OP
Ligand PG4 2 x PG4
Ligand PEG 3 x PEG
Ligand NHE 1 x NHE
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 93.247Å b: 98.847Å c: 140.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.174
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Medicinal chemistry advances in targeting class I histone deacetylases.
Abdallah et al. (2023)