Research workbench
Estrogen receptor in complex with proline-flanked lxxll peptides
Analyse Estrogen receptor in complex with proline-flanked lxxll peptides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J26
- Type
- protein
- Length
- 479 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor beta; 12-mer peptide
- UniProt
- Q92731
- Ligands
- EST
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 70% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor beta | protein | 228 | 70% helix, 4% strand | Q92731 |
| I | 12-mer peptide | protein | 12 | 67% helix, 0% strand | — |
| B | Estrogen receptor beta | protein | 229 | 69% helix, 3% strand | Q92731 |
| J | 12-mer peptide | protein | 10 | 80% helix, 0% strand | — |
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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.84 | 0.98 | 21 | EST |
| 2 | 167 | 0.83 | 0.98 | 22 | EST |
| 3 | 572 | 0.73 | 0.80 | 52 | empty |
| 4 | 130 | 0.62 | 0.86 | 23 | empty |
| 5 | 136 | 0.61 | 0.85 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1152 Ų buried · 13 hydrogen bonds · protein-protein
- A–I · 578 Ų buried · 8 hydrogen bonds · protein-protein
- B–J · 563 Ų buried · 6 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 4J26 · PDBe 4J26 · UniProt Q92731
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