PDBe 2vqj

X-ray diffraction
2.1Å resolution

Structure of HDAC4 catalytic domain bound to a trifluoromethylketone inhbitor

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 4 Chain: A
Molecule details ›
Chain: A
Length: 413 amino acids
Theoretical weight: 44.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56524 (Residues: 648-1057; Coverage: 38%)
Gene names: HDAC4, KIAA0288
Sequence domains: Histone deacetylase domain
Structure domains: Arginase; Chain A

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 106.77Å b: 137.562Å c: 68.993Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.225 0.276
Expression system: Escherichia coli BL21(DE3)