MolNFT v1 · #95829 · protein
Estrogen receptor in complex with proline-flanked lxxll peptides
4J24 · Estrogen receptor beta: “Estrogen receptor in complex with proline-flanked lxxll peptides”. X-ray diffraction, 1 ligand (EST), 17 pockets (best druggability 0.85). MolNFT v1 #95829 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4J24
- Type
- protein
- Length
- 944 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor beta; 19-mer peptide
- UniProt
- Q92731
- Ligands
- EST
- Pockets
- 17 · best druggability 0.85
Structure
x-ray diffraction · 6 distinct chains · 71% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Estrogen receptor beta | protein | 225 | 72% helix, 4% strand | Q92731 |
| B | Estrogen receptor beta | protein | 228 | 71% helix, 5% strand | Q92731 |
| D | Estrogen receptor beta | protein | 221 | 71% helix, 4% strand | Q92731 |
| K, I | 19-mer peptide | protein | 12 | 67% helix, 0% strand | — |
| J | 19-mer peptide | protein | 11 | 73% helix, 0% strand | — |
| L | 19-mer peptide | protein | 10 | 70% helix, 0% strand | — |
Ligands and binding sites
- EST · Estradiol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.85 | 0.98 | 23 | EST |
| 2 | 188 | 0.84 | 0.98 | 22 | EST |
| 3 | 180 | 0.84 | 0.97 | 21 | EST |
| 4 | 179 | 0.84 | 0.97 | 21 | EST |
| 5 | 641 | 0.76 | 0.82 | 86 | empty |
Interfaces
8 interfaces between chains.
- A–B · 1279 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1175 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 599 Ų buried · 4 hydrogen bonds · protein-protein
- A–I · 585 Ų buried · 9 hydrogen bonds · protein-protein
- C–K · 550 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 4J24 · PDBe 4J24 · UniProt Q92731
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