› 5di7

X-ray diffraction
2.24Å resolution

Crystal Structure of the ER-alpha Ligand-binding Domain in complex with an methyl-substituted A-CD ring estrogen derivative (1S,3aR,5S,7aS)-5-(4-hydroxy-2-methylphenyl)-7a-methyloctahydro-1H-inden-1-ol

Released:
DOI: 10.2210/pdb5di7/pdb
PDB entry 5di7 coloured by chain, front view.
PDB entry 5di7 coloured by chain, side view.
PDB entry 5di7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Predictive features of ligand-specific signaling through the estrogen receptor.
Nwachukwu JC, Srinivasan S, Zheng Y, Wang S, Min J, Dong C, Liao Z, Nowak J, Wright NJ, Houtman R, Carlson KE, Josan JS, Elemento O, Katzenellenbogen JA, Zhou HB, Nettles KW
Mol Syst Biol 12 864 (2016)
PMID: 27107013

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: 14 amino acids
Theoretical weight: 1.67 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15596 (Residues: 686-699; Coverage: 1%)
Gene names: BHLHE75, NCOA2, SRC2, TIF2

Ligands and Environments

1 bound ligand:
Ligand 5CQ 2 x 5CQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 55.962Å b: 83.298Å c: 58.536Å
α: 90° β: 109.44° γ: 90°
R-values:
R R work R free
0.178 0.175 0.213
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

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

1 mention without citation

Predictive features of ligand-specific signaling through the estrogen receptor.
Nwachukwu et al. (2016)