PDBe 4g1y

X-ray diffraction
2.85Å resolution

Structural basis for the accommodation of bis- and tris-aromatic derivatives in Vitamin D Nuclear Receptor

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vitamin D3 receptor A Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 33.92 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PTN2 (Residues: 156-453; Coverage: 66%)
Gene names: nr1i1a, vdr, vdra
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor coactivator 1 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.78 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15788 (Residues: 686-700; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P6522
Unit cell:
a: 65.559Å b: 65.559Å c: 263.876Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.27
Expression systems:
  • Escherichia coli
  • Not provided