› 1c3p

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF AN HDAC HOMOLOG FROM AQUIFEX AEOLICUS

Released:
DOI: 10.2210/pdb1c3p/pdb
PDB entry 1c3p coloured by chain, front view.
PDB entry 1c3p coloured by chain, side view.
PDB entry 1c3p 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: 42.73 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 51.4Å b: 93.8Å c: 78.7Å
α: 90° β: 96.9° γ: 90°
R-values:
R R work R free
0.198 0.198 0.24
Expression system: Escherichia coli

Quick links

Citations

270 review citations

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

12 mentions without citation

Evolution of the arginase fold and functional diversity.
Dowling et al. (2008)
11 more