› 4qa2

X-ray diffraction
2.38Å resolution

Crystal structure of I243N HDAC8 in complex with SAHA

Released:
DOI: 10.2210/pdb4qa2/pdb
PDB entry 4qa2 coloured by chain, front view.
PDB entry 4qa2 coloured by chain, side view.
PDB entry 4qa2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Compromised structure and function of HDAC8 mutants identified in Cornelia de Lange Syndrome spectrum disorders.
Decroos C, Bowman CM, Moser JA, Christianson KE, Deardorff MA, Christianson DW
ACS Chem Biol 9 2157-64 (2014)
PMID: 25075551

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-189815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 43.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BY41 (Residues: 1-377; Coverage: 100%)
Gene names: CDA07, HDAC8, HDACL1
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments

4 bound ligands:
Ligand K 4 x K
Ligand ZN 2 x ZN
Ligand SHH 2 x SHH
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 53.017Å b: 84.057Å c: 94.381Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.173 0.17 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

HDAC8: a multifaceted target for therapeutic interventions.
Chakrabarti et al. (2015)
12 more

4 mentions without citation

Structure-Based Inhibitor Discovery of Class I Histone Deacetylases (HDACs).
Luo et al. (2020)
3 more