MolNFT v1 · #145230 · protein
Estrogen receptor alpha Y537S covalently bound to antagonist H3B-5942.
6CHW: “Estrogen receptor alpha Y537S covalently bound to antagonist H3B-5942.”. X-ray diffraction, 1 ligand (F3D), 2 pockets (best druggability 0.75). MolNFT v1 #145230 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6CHW
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor
- UniProt
- P03372
- Ligands
- F3D
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 246 | 66% helix, 4% strand | P03372 |
Ligands and binding sites
- F3D · 4-[(2-{4-[(1E)-1-(1H-indazol-5-yl)-2-phenylbut-1-en-1-yl]phenoxy}ethyl)amino]-N,N-dimethylbutanamide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 443 | 0.75 | 0.84 | 41 | F3D, EDO |
| 2 | 99 | 0.62 | 0.88 | 21 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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
- Elsewhere: RCSB PDB 6CHW · PDBe 6CHW · UniProt P03372
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