PDBe 5h1e

X-ray diffraction
2.6Å resolution

Interaction between vitamin D receptor and coactivator peptide SRC2-3

Released:
Source organisms:
Primary publication:
SRC2-3 binds to vitamin D receptor with high sensitivity and strong affinity.
Bioorg. Med. Chem. 25 568-574 (2017)
PMID: 27890450

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vitamin D3 receptor Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 30.6 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13053 (Residues: 116-423; Coverage: 62%)
Gene names: Nr1i1, Vdr
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Nuclear receptor coactivator 2 Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.59 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15596 (Residues: 740-752; Coverage: 1%)
Gene names: BHLHE75, NCOA2, SRC2, TIF2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2
Unit cell:
a: 155.77Å b: 42.88Å c: 42.21Å
α: 90° β: 95.83° γ: 90°
R-values:
R R work R free
0.24 0.239 0.248
Expression systems:
  • Escherichia coli
  • Not provided