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Estrogen receptor alpha ligand binding domain in complex with RU39411
Analyse Estrogen receptor alpha ligand binding domain in complex with RU39411 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UJO
- Type
- protein
- Length
- 938 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor
- UniProt
- P03372
- Ligands
- QYM, MG
- Pockets
- 15 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Estrogen receptor | protein | 234 | 66% helix, 4% strand | P03372 |
| D | Estrogen receptor | protein | 240 | 66% helix, 4% strand | P03372 |
| C | Estrogen receptor | protein | 233 | 65% helix, 4% strand | P03372 |
| A | Estrogen receptor | protein | 231 | 67% helix, 4% strand | P03372 |
Ligands and binding sites
- QYM · (9beta,11beta,17beta)-11-{4-[2-(dimethylamino) ethoxy]phenyl}estra-1,3,5(10)-triene-3,17-diol · ligand · 4 copies · chains B, D, C, A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.85 | 0.86 | 131 | QYM |
| 2 | 238 | 0.83 | 0.95 | 33 | QYM |
| 3 | 281 | 0.80 | 0.91 | 36 | QYM |
| 4 | 102 | 0.65 | 0.89 | 20 | empty |
| 5 | 105 | 0.65 | 0.89 | 19 | empty |
Interfaces
4 interfaces between chains.
- B–A · 1572 Ų buried · 27 hydrogen bonds · protein-protein
- D–C · 647 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 307 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 264 Ų buried · 1 hydrogen bond · 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 P03372
- Elsewhere: RCSB PDB 7UJO · PDBe 7UJO · UniProt P03372
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