PDBe 3c10

X-ray diffraction
2Å resolution

Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 7 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 423 amino acids
Theoretical weight: 45.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WUI4 (Residues: 482-903; Coverage: 44%)
  • Best match: Q8WUI4-9 (Residues: 1-376)
Gene names: HDAC7, HDAC7A
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P32
Unit cell:
a: 81.827Å b: 81.827Å c: 148.97Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.201 0.263
Expression system: Escherichia coli BL21(DE3)