MolNFT v1 · #27039 · protein
Crystal structure of estrogen receptor alpha complexed with genistein
1X7R · Estrogen receptor 1 (alpha): “Crystal structure of estrogen receptor alpha complexed with genistein”. X-ray diffraction, 1 ligand (GEN), 2 pockets (best druggability 0.82). MolNFT v1 #27039 on GenesisL1: 3D structure, binding sites…
- PDB
- 1X7R
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor 1 (alpha); Steroid receptor coactivator-3
- UniProt
- P03372
- Ligands
- GEN
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor 1 (alpha) | protein | 235 | 73% helix, 4% strand | P03372 |
| B | Steroid receptor coactivator-3 | protein | 9 | 78% helix, 0% strand | — |
Ligands and binding sites
- GEN · Genistein · ligand · chains A
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 | 171 | 0.82 | 0.97 | 22 | GEN |
| 2 | 136 | 0.61 | 0.85 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 486 Ų buried · 7 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 P03372
- Elsewhere: RCSB PDB 1X7R · PDBe 1X7R · UniProt P03372
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