› 1yin

X-ray diffraction
2.2Å resolution

Human estrogen receptor alpha ligand-binding domain in complex with compound 3F

Released:
DOI: 10.2210/pdb1yin/pdb
PDB entry 1yin coloured by chain, front view.
PDB entry 1yin coloured by chain, side view.
PDB entry 1yin coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Estrogen receptor ligands. Part 10: Chromanes: old scaffolds for new SERAMs.
Tan Q, Blizzard TA, Morgan JD, Birzin ET, Chan W, Yang YT, Pai LY, Hayes EC, DaSilva CA, Warrier S, Yudkovitz J, Wilkinson HA, Sharma N, Fitzgerald PM, Li S, Colwell L, Fisher JE, Adamski S, Reszka AA, Kimmel D, DiNinno F, Rohrer SP, Freedman LP, Schaeffer JM, Hammond ML
Bioorg Med Chem Lett 15 1675-81 (2005)
PMID: 15745820

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: 248 amino acids
Theoretical weight: 28.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03372 (Residues: 307-554; Coverage: 42%)
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 CM3 1 x CM3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6522
Unit cell:
a: 58.85Å b: 58.85Å c: 277.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 not available 0.296
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Estrogen receptors: how do they signal and what are their targets.
Heldring et al. (2007)
3 more

8 mentions without citation

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