› 1g50

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1g50/pdb
PDB entry 1g50 coloured by chain, front view.
PDB entry 1g50 coloured by chain, side view.
PDB entry 1g50 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Overexpression, purification, and crystal structure of native ER alpha LBD.
Eiler S, Gangloff M, Duclaud S, Moras D, Ruff M
Protein Expr Purif 22 165-73 (2001)
PMID: 11437591

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136919 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Estrogen receptor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 247 amino acids
Theoretical weight: 28.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03372 (Residues: 304-550; 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 EST 3 x EST
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P3221
Unit cell:
a: 105.5Å b: 105.5Å c: 136.08Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.241 0.241 0.31
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

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

21 mentions without citation

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