› 1l2i

X-ray diffraction
1.95Å resolution

Human Estrogen Receptor alpha Ligand-binding Domain in Complex with (R,R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol and a Glucocorticoid Receptor Interacting Protein 1 NR box II Peptide

Released:
DOI: 10.2210/pdb1l2i/pdb
PDB entry 1l2i coloured by chain, front view.
PDB entry 1l2i coloured by chain, side view.
PDB entry 1l2i coloured by chain, top view.
Source organisms:
Primary publication:
Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism.
Shiau AK, Barstad D, Radek JT, Meyers MJ, Nettles KW, Katzenellenbogen BS, Katzenellenbogen JA, Agard DA, Greene GL
Nat Struct Biol 9 359-64 (2002)
PMID: 11953755

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136930 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Estrogen receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 29.91 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
Nuclear receptor coactivator 2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 13 amino acids
Theoretical weight: 1.58 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q61026 (Residues: 686-698; Coverage: 1%)
Gene names: Grip1, Ncoa2, Src2, Tif2

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand ETC 2 x ETC
1 modified residue:
Ligand CCS 2 x CCS

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 54.545Å b: 82.6Å c: 59.04Å
α: 90° β: 111.53° γ: 90°
R-values:
R R work R free
0.203 0.203 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

40 review citations

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

35 mentions without citation

Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance.
Katzenellenbogen et al. (2018)
34 more