› 1c3s

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF AN HDAC HOMOLOG COMPLEXED WITH SAHA

Released:
DOI: 10.2210/pdb1c3s/pdb
PDB entry 1c3s coloured by chain, front view.
PDB entry 1c3s coloured by chain, side view.
PDB entry 1c3s coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors.
Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, Breslow R, Pavletich NP
Nature 401 188-93 (1999)
PMID: 10490031

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetoin utilization protein AcuC Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 42.7 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67135 (Residues: 1-375; Coverage: 100%)
Gene names: acuC1, aq_1023
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand SHH 1 x SHH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 51.495Å b: 94.155Å c: 78.977Å
α: 90° β: 97.024° γ: 90°
R-values:
R R work R free
0.2 0.2 0.277
Expression system: Escherichia coli

Quick links

Citations

271 review citations

Histone deacetylases (HDACs): characterization of the classical HDAC family.
de Ruijter et al. (2003)
270 more

12 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
11 more