› 2qab

X-ray diffraction
1.89Å resolution

Crystal Structure of Estrogen Receptor Alpha Ligand Binding Domain Mutant 537S Complexed with an Ethyl Indazole Compound

Released:
DOI: 10.2210/pdb2qab/pdb
PDB entry 2qab coloured by chain, front view.
PDB entry 2qab coloured by chain, side view.
PDB entry 2qab coloured by chain, top view.
Source organisms:
Primary publication:
NFkappaB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses.
Nettles KW, Bruning JB, Gil G, Nowak J, Sharma SK, Hahm JB, Kulp K, Hochberg RB, Zhou H, Katzenellenbogen JA, Katzenellenbogen BS, Kim Y, Joachmiak A, Greene GL
Nat Chem Biol 4 241-7 (2008)
PMID: 18344977

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Estrogen receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 29.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03372 (Residues: 298-554; 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

1 bound ligand:
Ligand EI1 2 x EI1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 55.824Å b: 83.08Å c: 58.304Å
α: 90° β: 109.13° γ: 90°
R-values:
R R work R free
0.226 0.224 0.27
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

15 review citations

ESR1 mutations—a mechanism for acquired endocrine resistance in breast cancer.
Jeselsohn et al. (2015)
14 more

4 mentions without citation

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