› 2vqw

X-ray diffraction
3Å resolution

Structure of inhibitor-free HDAC4 catalytic domain (with gain-of- function mutation His332Tyr)

Released:
DOI: 10.2210/pdb2vqw/pdb
PDB entry 2vqw coloured by chain, front view.
PDB entry 2vqw coloured by chain, side view.
PDB entry 2vqw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain.
Bottomley MJ, Lo Surdo P, Di Giovine P, Cirillo A, Scarpelli R, Ferrigno F, Jones P, Neddermann P, De Francesco R, Steinkühler C, Gallinari P, Carfí A
J Biol Chem 283 26694-704 (2008)
PMID: 18614528

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 4 Chain: G
Molecule details ›
Chain: G
Length: 413 amino acids
Theoretical weight: 44.5 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: Histone deacetylase domain

Ligands and Environments

2 bound ligands:
Ligand K 2 x K
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 137.911Å b: 137.911Å c: 69.519Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.233 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

55 review citations

The many roles of histone deacetylases in development and physiology: implications for disease and therapy.
Haberland et al. (2009)
54 more

10 mentions without citation

Erasers of histone acetylation: the histone deacetylase enzymes.
Seto et al. (2014)
9 more