Research workbench
Wild type estrogen nuclear receptor ligand binding domain complexed with estradiol
Analyse Wild type estrogen nuclear receptor ligand binding domain complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QKU
- Type
- protein
- Length
- 744 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estradiol receptor
- UniProt
- P03372
- Ligands
- EST
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estradiol receptor | protein | 250 | 65% helix, 2% strand | P03372 |
| B, C | Estradiol receptor | protein | 247 | 66% helix, 2% strand | P03372 |
Ligands and binding sites
- EST · Estradiol · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.85 | 0.98 | 23 | EST |
| 2 | 194 | 0.85 | 0.98 | 25 | EST |
| 3 | 194 | 0.85 | 0.98 | 25 | EST |
| 4 | 491 | 0.67 | 0.78 | 52 | empty |
| 5 | 460 | 0.63 | 0.77 | 41 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1905 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 171 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1QKU · Wild type estrogen nuclear receptor ligand binding domain complexed with estradiol · the same entry in another collection · chain A against A, TM-score 1.00
- P03372 · AlphaFold monomer V2.0 prediction for estrogen receptor (P03372) · a predicted model of the same protein · chain C against A, TM-score 0.97
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 1QKU · PDBe 1QKU · UniProt P03372
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