Research workbench
Estrogen receptor alpha in complex with a stabilized peptide antagonist 6
Analyse Estrogen receptor alpha in complex with a stabilized peptide antagonist 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GTR
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Arg-ias-ile-0JY-dpp-arg-0JY-0JY-gln-NH2
- UniProt
- P03372
- Ligands
- EST, NH2
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 236 | 73% helix, 4% strand | P03372 |
| C | Arg-ias-ile-0JY-dpp-arg-0JY-0JY-gln-NH2 | protein | 9 | 56% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.84 | 0.98 | 22 | EST |
| 2 | 93 | 0.65 | 0.90 | 19 | empty |
| 3 | 53 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–C · 434 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (nonstandard).
Compared structures
- 5GTR · estrogen receptor alpha in complex with a stabilized peptide antagonist 6 · the same entry in another collection · chain A against A, TM-score 1.00
- P03372 · AlphaFold monomer V2.0 prediction for estrogen receptor (P03372) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 5GTR · PDBe 5GTR · UniProt P03372
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