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Crystal structure of the er-alpha ligand-binding domain (L372S, L536S) in complex with dmeri-21
Analyse Crystal structure of the er-alpha ligand-binding domain (L372S, L536S) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RS1
- Type
- protein
- Length
- 912 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor
- UniProt
- P03372
- Ligands
- 7Q5
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 231 | 72% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 221 | 72% helix, 4% strand | P03372 |
| C | Estrogen receptor | protein | 233 | 71% helix, 4% strand | P03372 |
| D | Estrogen receptor | protein | 227 | 71% helix, 4% strand | P03372 |
Ligands and binding sites
- 7Q5 · methyl 3-(4-{[(1S,2R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hept-5-ene-2-sulfonyl](2,2,2-trifluoroethyl)amino}phenyl)prop-2-enoate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.81 | 0.91 | 27 | 7Q5 |
| 2 | 316 | 0.80 | 0.90 | 30 | 7Q5 |
| 3 | 296 | 0.79 | 0.90 | 30 | 7Q5 |
| 4 | 351 | 0.76 | 0.86 | 35 | 7Q5 |
| 5 | 588 | 0.66 | 0.76 | 62 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1607 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 1592 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 286 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (alkylation).
Compared structures
- 7RS1 · Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with… · the same entry in another collection · chain D against D, 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 0.93
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 P03372
- Elsewhere: RCSB PDB 7RS1 · PDBe 7RS1 · UniProt P03372
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