› 4j26

X-ray diffraction
2.3Å resolution

Estrogen Receptor in complex with proline-flanked LXXLL peptides

Released:
DOI: 10.2210/pdb4j26/pdb
PDB entry 4j26 coloured by chain, front view.
PDB entry 4j26 coloured by chain, side view.
PDB entry 4j26 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Proline primed helix length as a modulator of the nuclear receptor-coactivator interaction.
Fuchs S, Nguyen HD, Phan TT, Burton MF, Nieto L, de Vries-van Leeuwen IJ, Schmidt A, Goodarzifard M, Agten SM, Rose R, Ottmann C, Milroy LG, Brunsveld L
J Am Chem Soc 135 4364-71 (2013)
PMID: 23437920

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164597 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Estrogen receptor beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 27.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92731 (Residues: 261-500; Coverage: 45%)
Gene names: ESR2, ESTRB, NR3A2
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
12-mer Peptide Chains: I, J
Molecule details ›
Chains: I, J
Length: 12 amino acids
Theoretical weight: 1.45 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand EST 2 x EST
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P32
Unit cell:
a: 62.63Å b: 62.63Å c: 125.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.242
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Modulating protein-protein interactions: the potential of peptides.
Nevola et al. (2015)
4 more

2 mentions without citation

Network pharmacology-based analysis for unraveling potential cancer-related molecular targets of Egyptian propolis phytoconstituents accompanied with molecular docking and in vitro studies.
Ibrahim et al. (2021)
1 more