Research workbench
Crystal structure of estrogen receptor beta complexed with 3-bromo-6-hydroxy-2-(4-hydroxy-phenyl)-inden-1-one
Analyse Crystal structure of estrogen receptor beta complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZAF
- Type
- protein
- Length
- 482 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor beta; Nuclear receptor coactivator 1
- EC
- 2.3.1.48
- UniProt
- Q92731, Q15788
- Ligands
- 789
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Estrogen receptor beta | protein | 228 | 70% helix, 3% strand | Q92731 |
| C, D | Nuclear receptor coactivator 1 (EC 2.3.1.48) | protein | 13 | 46% helix, 0% strand | Q15788 |
Ligands and binding sites
- 789 · 3-bromo-6-hydroxy-2-(4-hydroxyphenyl)-1H-inden-1-one · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.83 | 0.98 | 21 | 789 |
| 2 | 160 | 0.81 | 0.96 | 21 | 789 |
| 3 | 81 | 0.67 | 0.93 | 21 | empty |
| 4 | 551 | 0.65 | 0.76 | 49 | empty |
| 5 | 133 | 0.62 | 0.86 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1347 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 578 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 513 Ų buried · 4 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
- Every structure of UniProt Q15788
- Elsewhere: RCSB PDB 1ZAF · PDBe 1ZAF · UniProt Q92731 · UniProt Q15788
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