PDBe 4bkx

X-ray diffraction
3Å resolution

The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Metastasis-associated protein MTA1 Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 19.96 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: NEW Q13330 (Residues: 162-335; Coverage: 24%)
Gene name: MTA1
Sequence domains:
Structure domains:
Histone deacetylase 1 Chain: B
Molecule details ›
Chain: B
Length: 482 amino acids
Theoretical weight: 55.18 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: NEW Q13547 (Residues: 1-482; Coverage: 100%)
Gene names: HDAC1, RPD3L1
Sequence domains: Histone deacetylase domain
Structure domains: Histone deacetylase domain

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P3221
Unit cell:
a: 108.199Å b: 108.199Å c: 133.164Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.211 0.261
Expression system: Homo sapiens