MolNFT v1 · #13145 · protein
Human estrogen receptor beta ligand-binding domain in complex with (R, R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol
1L2J: “Human estrogen receptor beta ligand-binding domain in complex with (R…”. X-ray diffraction, 1 ligand (ETC), 6 pockets (best druggability 0.81). MolNFT v1 #13145 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1L2J
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor beta
- UniProt
- Q92731
- Ligands
- ETC
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor beta | protein | 232 | 71% helix, 2% strand | Q92731 |
| B | Estrogen receptor beta | protein | 223 | 72% helix, 2% strand | Q92731 |
Ligands and binding sites
- ETC · (R,R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.81 | 0.90 | 40 | ETC |
| 2 | 294 | 0.77 | 0.88 | 35 | ETC |
| 3 | 97 | 0.69 | 0.93 | 17 | empty |
| 4 | 130 | 0.66 | 0.88 | 20 | empty |
| 5 | 65 | 0.32 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 76 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1L2J · Human Estrogen Receptor beta Ligand-binding Domain in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92731 · AlphaFold monomer V2.0 prediction for estrogen receptor beta (Q92731) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 1L2J · PDBe 1L2J · UniProt Q92731
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