› 4q13

X-ray diffraction
2.24Å resolution

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: 261 amino acids
Theoretical weight: 29.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03372 (Residues: 299-554; 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: synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: Q15596 (Residues: 686-698; Coverage: 1%)
Gene names: BHLHE75, NCOA2, SRC2, TIF2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 56.14Å b: 82.655Å c: 59.113Å
α: 90° β: 111.05° γ: 90°
R-values:
R R work R free
0.201 0.198 0.249
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

48 review citations

Epigenetic mechanisms in breast cancer therapy and resistance.
Garcia-Martinez et al. (2021)
47 more

97 mentions without citation

Clinical, genetic and imaging findings identify new causes for corpus callosum development syndromes.
Edwards et al. (2014)
96 more