› 1vkg

X-ray diffraction
2.2Å resolution

Crystal Structure of Human HDAC8 complexed with CRA-19156

Released:
DOI: 10.2210/pdb1vkg/pdb
PDB entry 1vkg coloured by chain, front view.
PDB entry 1vkg coloured by chain, side view.
PDB entry 1vkg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases.
Somoza JR, Skene RJ, Katz BA, Mol C, Ho JD, Jennings AJ, Luong C, Arvai A, Buggy JJ, Chi E, Tang J, Sang BC, Verner E, Wynands R, Leahy EM, Dougan DR, Snell G, Navre M, Knuth MW, Swanson RV, McRee DE, Tari LW
Structure 12 1325-34 (2004)
PMID: 15242608

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 377 amino acids
Theoretical weight: 41.8 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
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

3 bound ligands:
Ligand ZN 2 x ZN
Ligand NA 2 x NA
Ligand CRI 2 x CRI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 82.63Å b: 92.71Å c: 98.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.304
Expression system: Spodoptera frugiperda

Quick links

Citations

108 review citations

Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer.
Minucci et al. (2006)
107 more

28 mentions without citation

HDAC8 substrates: Histones and beyond.
Wolfson et al. (2013)
27 more