› 2yat

X-ray diffraction
2.6Å resolution

Crystal structure of estradiol derived metal chelate and estrogen receptor-ligand binding domain complex

Released:
DOI: 10.2210/pdb2yat/pdb
PDB entry 2yat coloured by chain, front view.
PDB entry 2yat coloured by chain, side view.
PDB entry 2yat coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of estradiol metal chelate and estrogen receptor complex: the basis for designing a new class of selective estrogen receptor modulators.
Li MJ, Greenblatt HM, Dym O, Albeck S, Pais A, Gunanathan C, Milstein D, Degani H, Sussman JL
J Med Chem 54 3575-80 (2011)
PMID: 21473635

Function and Biology Details

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

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: 252 amino acids
Theoretical weight: 28.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03372 (Residues: 301-551; Coverage: 42%)
Gene names: ESR, ESR1, NR3A1
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

3 bound ligands:
Ligand EU 1 x EU
Ligand EEU 1 x EEU
Ligand FMT 2 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3212
Unit cell:
a: 64.693Å b: 64.693Å c: 133.345Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Nuclear and extranuclear-initiated estrogen receptor signaling crosstalk and endocrine resistance in breast cancer.
Kulkoyluoglu et al. (2016)
7 other articles

6 mentions without citation

Versatility or promiscuity: the estrogen receptors, control of ligand selectivity and an update on subtype selective ligands.
Ng et al. (2014)
5 more