Crystal Structure of the Androgen Receptor Ligand Binding Domain (LBD) with DHT and a peptide derived from its physiological coactivator ARA70. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Jan 2005.
Explore 1T5Z in 3D Show helices and sheets RCSB PDB PDBe
1T5Z contains 16 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 672-680 | 9 | |
| α-helix | 694-695 | 2 | |
| α-helix | 697-720 | 24 | |
| α-helix | 725-727 | 3 | |
| α-helix | 730-757 | 28 | |
| β-strand | 762-765 | 4 | 1 |
| β-strand | 768-770 | 3 | 1 |
| α-helix | 772-777 | 6 | |
| α-helix | 781-796 | 16 | |
| α-helix | 801-810 | 10 | |
| α-helix | 811-813 | 3 | |
| β-strand | 815-817 | 3 | 2 |
| α-helix | 824-843 | 20 | |
| α-helix | 849-864 | 16 | |
| α-helix | 866-882 | 17 | |
| α-helix | 884-887 | 4 | |
| α-helix | 893-901 | 9 | |
| α-helix | 903-907 | 5 | |
| β-strand | 911-913 | 3 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 922-928 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Androgen receptor | A | protein | 251 | Homo sapiens | P10275 (AlphaFold model) |
| Nuclear receptor coactivator 4 | B | protein | 15 | Homo sapiens | Q13772 (AlphaFold model) |
>1T5Z_1 Androgen receptor (chains A) CQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNL HVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMR HLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKN PTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILS GKVKPIYFHTQ
>1T5Z_2 Nuclear receptor coactivator 4 (chains B) RETSEKFKLLFQSYN
| ID | Name | Formula | Copies |
|---|---|---|---|
| DHT | 5-alpha-dihydrotestosterone | C19 H30 O2 | 1 |
The Molecular Mechanisms of Coactivator Utilization in Ligand-dependent Transactivation by the Androgen Receptor. Estebanez-Perpina, E., Moore, J.M.R., Mar, E. et al. J Biol Chem (2005) 280:8060-8068. DOI 10.1074/jbc.M407046200 · PubMed
Other PDB entries of the same protein (UniProt P10275 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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