› 1t79

X-ray diffraction
1.8Å resolution

Crystal structure of the androgen receptor ligand binding domain in complex with a FxxLW motif

Released:
DOI: 10.2210/pdb1t79/pdb
PDB entry 1t79 coloured by chain, front view.
PDB entry 1t79 coloured by chain, side view.
PDB entry 1t79 coloured by chain, top view.
Source organism: Pan troglodytes
Primary publication:
Recognition and accommodation at the androgen receptor coactivator binding interface.
Hur E, Pfaff SJ, Payne ES, Grøn H, Buehrer BM, Fletterick RJ
OpenAccess logo PLoS Biol 2 E274 (2004)
PMID: 15328534

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-523252 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Androgen receptor Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 30.88 KDa
Source organism: Pan troglodytes
Expression system: Escherichia coli
UniProt:
  • Canonical: O97775 (Residues: 654-911; Coverage: 28%)
Gene names: AR, NR3C4
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
FxxLW motif peptide Chain: B
Molecule details ›
Chain: B
Length: 20 amino acids
Theoretical weight: 2.12 KDa
Source organism: Pan troglodytes
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand DHT 1 x DHT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 55.826Å b: 66.128Å c: 68.381Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.234
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

30 review citations

Androgen receptor: structure, role in prostate cancer and drug discovery.
Tan et al. (2015)
29 more

3 mentions without citation

Recognition and accommodation at the androgen receptor coactivator binding interface.
Hur et al. (2004)
2 more