› 2qa8

X-ray diffraction
1.85Å resolution

Crystal Structure of the Estrogen Receptor Alpha Ligand Binding Domain Mutant 537S Complexed with Genistein

Released:
DOI: 10.2210/pdb2qa8/pdb
PDB entry 2qa8 coloured by chain, front view.
PDB entry 2qa8 coloured by chain, side view.
PDB entry 2qa8 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-136911 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Estrogen receptor Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 29.46 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
Estrogen receptor Chain: B
Molecule details ›
Chain: B
Length: 258 amino acids
Theoretical weight: 29.46 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 GEN 2 x GEN
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 55.668Å b: 77.957Å c: 58Å
α: 90° β: 109.05° γ: 90°
R-values:
R R work R free
0.214 0.211 0.264
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

16 review citations

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

11 mentions without citation

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