MolNFT v1 · #81551 · protein
Crystal structure of hera-lbd (Y537S) in complex with bisphenol-a
3UU7 · Estrogen receptor: “Crystal structure of hera-lbd (Y537S) in complex with bisphenol-a”. X-ray diffraction, 1 ligand (2OH), 6 pockets (best druggability 0.84). MolNFT v1 #81551 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3UU7
- Type
- protein
- Length
- 492 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Nuclear receptor coactivator 1
- EC
- 2.3.1.48
- UniProt
- P03372, Q15788
- Ligands
- 2OH
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 239 | 69% helix, 3% strand | P03372 |
| B | Estrogen receptor | protein | 235 | 68% helix, 4% strand | P03372 |
| F, G | Nuclear receptor coactivator 1 (EC 2.3.1.48) | protein | 9 | 78% helix, 0% strand | Q15788 |
Ligands and binding sites
- 2OH · 4,4'-propane-2,2-diyldiphenol · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.84 | 0.98 | 21 | 2OH |
| 2 | 168 | 0.83 | 0.97 | 21 | 2OH |
| 3 | 91 | 0.65 | 0.90 | 21 | empty |
| 4 | 95 | 0.65 | 0.90 | 18 | empty |
| 5 | 393 | 0.60 | 0.76 | 49 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1663 Ų buried · 23 hydrogen bonds · protein-protein
- B–G · 496 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 466 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (oxidation).
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
- Every structure of UniProt Q15788
- Elsewhere: RCSB PDB 3UU7 · PDBe 3UU7 · UniProt P03372 · UniProt Q15788
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