Research workbench
Crystal structure of the androgen receptor ligand binding domain with dht and a peptide derived form its physiological coactivator GRIP1 nr box 2 bound in a non-helical conformation
Analyse Crystal structure of the androgen receptor ligand binding domain with dht and a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T65
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Androgen receptor; Nuclear receptor coactivator 2
- UniProt
- P10275, Q15596
- Ligands
- DHT
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Androgen receptor | protein | 251 | 67% helix, 5% strand | P10275 |
| B | Nuclear receptor coactivator 2 | protein | 7 | 0% helix, 0% strand | Q15596 |
Ligands and binding sites
- DHT · 5-alpha-dihydrotestosterone · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.84 | 0.98 | 24 | DHT |
| 2 | 156 | 0.63 | 0.85 | 26 | empty |
| 3 | 63 | 0.31 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 402 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1T65 · Crystal structure of the androgen receptor ligand binding domain with DHT and a peptide… · the same entry in another collection · chain A against A, TM-score 1.00
- P10275 · AlphaFold monomer V2.0 prediction for androgen receptor (P10275) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10275
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 1T65 · PDBe 1T65 · UniProt P10275 · UniProt Q15596
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