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
Sequence domain:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Histone deacetylase 4 (preferred)
PDBe Complex ID:
PDB-CPX-157484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 4
Molecule details ›
Chains: A, B, C, D
Length: 112 amino acids
Theoretical weight: 13.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Glutamine rich N terminal domain of histone deacetylase 4
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 112 amino acids
Theoretical weight: 13.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P56524 (Residues: 62-153; Coverage: 9%)
Sequence domains: Glutamine rich N terminal domain of histone deacetylase 4
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 8.2.1
Spacegroup:
C2
Expression system: Escherichia coli
