› 3mz4

X-ray diffraction
1.84Å resolution

Crystal structure of D101L Mn2+ HDAC8 complexed with M344

Released:
DOI: 10.2210/pdb3mz4/pdb
PDB entry 3mz4 coloured by chain, front view.
PDB entry 3mz4 coloured by chain, side view.
PDB entry 3mz4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function .
Dowling DP, Gattis SG, Fierke CA, Christianson DW
Biochemistry 49 5048-56 (2010)
PMID: 20545365

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
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 43.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

4 bound ligands:
Ligand MN 2 x MN
Ligand K 4 x K
Ligand B3N 2 x B3N
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 88.353Å b: 91.148Å c: 104.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.201 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

HDAC8: a multifaceted target for therapeutic interventions.
Chakrabarti et al. (2015)
16 more

6 mentions without citation

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