Research workbench
Crystal structure of the er-alpha ligand-binding domain in complex with the cyclofenil derivative 4,4'-{[4-(2-hydroxyethyl) CYCLOHEXYLIDENE]METHANEDIYL}DIPHENOL
Analyse Crystal structure of the er-alpha ligand-binding domain in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E15
- Type
- protein
- Length
- 469 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Nuclear receptor coactivator 2
- UniProt
- P03372
- Ligands
- 5KA
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 67% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 218 | 69% helix, 3% strand | P03372 |
| B | Estrogen receptor | protein | 233 | 67% helix, 4% strand | P03372 |
| C, D | Nuclear receptor coactivator 2 | protein | 9 | 44% helix, 0% strand | — |
Ligands and binding sites
- 5KA · 4,4'-({4-[2-(4-fluorobutoxy)ethyl]cyclohexylidene}methanediyl)diphenol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 343 | 0.81 | 0.90 | 39 | 5KA |
| 2 | 277 | 0.78 | 0.89 | 30 | 5KA |
| 3 | 84 | 0.63 | 0.90 | 16 | empty |
| 4 | 84 | 0.62 | 0.89 | 17 | empty |
| 5 | 205 | 0.48 | 0.75 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1652 Ų buried · 27 hydrogen bonds · protein-protein
- B–D · 498 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 469 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5E15 · Crystal Structure of the ER-alpha Ligand-binding Domain in Complex with the Cyclofenil… · 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 A against A, TM-score 0.98
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 5E15 · PDBe 5E15 · UniProt P03372
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