MolNFT v1 · #135085 · protein
Crystal structure of er beta bound to estradiol
5TOA · Estrogen receptor beta: “Crystal structure of er beta bound to estradiol”. X-ray diffraction, 1 ligand (EST), 7 pockets (best druggability 0.83). MolNFT v1 #135085 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TOA
- Type
- protein
- Length
- 462 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor beta
- UniProt
- Q92731
- Ligands
- EST
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor beta | protein | 230 | 70% helix, 4% strand | Q92731 |
| B | Estrogen receptor beta | protein | 232 | 67% helix, 5% strand | Q92731 |
Ligands and binding sites
- EST · Estradiol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.83 | 0.98 | 22 | EST |
| 2 | 155 | 0.83 | 0.98 | 21 | EST |
| 3 | 363 | 0.63 | 0.79 | 44 | empty |
| 4 | 130 | 0.62 | 0.86 | 21 | empty |
| 5 | 134 | 0.62 | 0.85 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1376 Ų buried · 15 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 Q92731
- Elsewhere: RCSB PDB 5TOA · PDBe 5TOA · UniProt Q92731
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