› 4qa1

X-ray diffraction
1.92Å resolution

Crystal structure of A188T HDAC8 in complex with M344

Released:
DOI: 10.2210/pdb4qa1/pdb
PDB entry 4qa1 coloured by chain, front view.
PDB entry 4qa1 coloured by chain, side view.
PDB entry 4qa1 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 8 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 389 amino acids
Theoretical weight: 43.26 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 8 x K
Ligand ZN 4 x ZN
Ligand B3N 4 x B3N
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 98.419Å b: 82.648Å c: 105.649Å
α: 90° β: 102.15° γ: 90°
R-values:
R R work R free
0.176 0.174 0.215
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

1 mention without citation

Preparation of a new construct of human histone deacetylase 8 for the crystallization of enzyme-inhibitor complexes.
Porter et al. (2019)