› 2am9

X-ray diffraction
1.64Å resolution

Crystal structure of human androgen receptor ligand binding domain in complex with testosterone

Released:
DOI: 10.2210/pdb2am9/pdb
PDB entry 2am9 coloured by chain, front view.
PDB entry 2am9 coloured by chain, side view.
PDB entry 2am9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity.
Pereira de Jésus-Tran K, Côté PL, Cantin L, Blanchet J, Labrie F, Breton R
Protein Sci 15 987-99 (2006)
PMID: 16641486

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Androgen receptor Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10275 (Residues: 655-920; Coverage: 29%)
Gene names: AR, DHTR, NR3C4
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

4 bound ligands:
Ligand SO4 1 x SO4
Ligand TES 1 x TES
Ligand DTT 1 x DTT
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 53.82Å b: 65.92Å c: 71.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.191 0.23
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Looking at nuclear receptors from a new angle.
Helsen et al. (2014)
23 more

64 mentions without citation

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