› 5tn6

X-ray diffraction
2.09Å resolution

Crystal Structure of the ER-alpha Ligand-binding Domain (Y537S) in Complex with the Spiro BC-estradiol, (1S,1'S,3a'S,7a'S)-7a'-methyl-1',2,2',3,3',3a',4',6',7',7a'-decahydro-1,5'-spirobi[indene]-1',5-diol

Released:
DOI: 10.2210/pdb5tn6/pdb
PDB entry 5tn6 coloured by chain, front view.
PDB entry 5tn6 coloured by chain, side view.
PDB entry 5tn6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Systems Structural Biology Analysis of Ligand Effects on ERα Predicts Cellular Response to Environmental Estrogens and Anti-hormone Therapies.
Nwachukwu JC, Srinivasan S, Bruno NE, Nowak J, Wright NJ, Minutolo F, Rangarajan ES, Izard T, Yao XQ, Grant BJ, Kojetin DJ, Elemento O, Katzenellenbogen JA, Nettles KW
Cell Chem Biol 24 35-45 (2017)
PMID: 28042045

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-136928 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Estrogen receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 29.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15596 (Residues: 686-698; Coverage: 1%)
Gene names: BHLHE75, NCOA2, SRC2, TIF2

Ligands and Environments

1 bound ligand:
Ligand 7G1 2 x 7G1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 56.02Å b: 82.85Å c: 58.97Å
α: 90° β: 110.89° γ: 90°
R-values:
R R work R free
0.195 0.192 0.225
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

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

1 mention without citation

CHARMM-GUI Ligand Designer for Template-Based Virtual Ligand Design in a Binding Site.
Guterres et al. (2021)