Research workbench
Crystal structure of ar-lbd bound with co-regulator peptide
Analyse Crystal structure of ar-lbd bound with co-regulator peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OEY
- Type
- protein
- Length
- 249 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Androgen receptor; Co-regulator peptide
- UniProt
- P10275
- Ligands
- DHT, SO4
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Androgen receptor | protein | 241 | 67% helix, 5% strand | P10275 |
| B | Co-regulator peptide | protein | 8 | 75% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.83 | 0.98 | 20 | DHT |
| 2 | 142 | 0.63 | 0.86 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 475 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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
- Elsewhere: RCSB PDB 4OEY · PDBe 4OEY · UniProt P10275
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