› 3f0r

X-ray diffraction
2.54Å resolution

Crystal Structure Analysis of Human HDAC8 complexed with trichostatin A in a new monoclinic crystal form

Released:
DOI: 10.2210/pdb3f0r/pdb
PDB entry 3f0r coloured by chain, front view.
PDB entry 3f0r coloured by chain, side view.
PDB entry 3f0r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors.
Dowling DP, Gantt SL, Gattis SG, Fierke CA, Christianson DW
Biochemistry 47 13554-63 (2008)
PMID: 19053282

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
Molecule details ›
Chains: A, B, C
Length: 388 amino acids
Theoretical weight: 43.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 3 x ZN
Ligand K 6 x K
Ligand TSN 6 x TSN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 87.895Å b: 90.705Å c: 92.141Å
α: 90° β: 94.63° γ: 90°
R-values:
R R work R free
0.21 0.21 0.258
Expression system: Escherichia coli

Quick links

Citations

20 review citations

HDACs and HDAC Inhibitors in Cancer Development and Therapy.
Li et al. (2016)
19 more

13 mentions without citation

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