› 3ert

X-ray diffraction
1.9Å resolution

HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH 4-HYDROXYTAMOXIFEN

Released:
DOI: 10.2210/pdb3ert/pdb
PDB entry 3ert coloured by chain, front view.
PDB entry 3ert coloured by chain, side view.
PDB entry 3ert coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen.
Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL
Cell 95 927-37 (1998)
PMID: 9875847

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136919 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Estrogen receptor Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03372 (Residues: 297-554; Coverage: 43%)
Gene names: ESR, ESR1, NR3A1
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand OHT 1 x OHT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6522
Unit cell:
a: 58.242Å b: 58.242Å c: 277.467Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.262
Expression system: Escherichia coli

Quick links

Citations

324 review citations

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Wright et al. (1999)
323 more

220 mentions without citation

Molecular mechanism of estrogen-estrogen receptor signaling.
Yaşar et al. (2017)
219 more