1ERE: Human estrogen receptor ligand-binding domain
Human estrogen receptor ligand-binding domain in complex with 17BETA-estradiol. Determined by X-ray diffraction at 3.1 Å resolution. Released 16 Sept 1998.
- Method
- X-ray diffraction
- Resolution
- 3.1 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 11,496
- Mol. weight
- 174.97 kDa
- Ligands
- EST
- Released
- 16 Sept 1998
Explore 1ERE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1ERE contains 75 α-helices and 12 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 312-322 | 11 | |
| α-helix | 324-327 | 4 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-394 | 23 | |
| β-strand | 401-405 | 5 | 1 |
| β-strand | 408-411 | 4 | 1 |
| α-helix | 412-417 | 6 | |
| α-helix | 421-437 | 17 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Chain B: 13 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 306-309 | 4 | |
| α-helix | 312-322 | 11 | |
| α-helix | 324-326 | 3 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-395 | 24 | |
| β-strand | 401-405 | 5 | 2 |
| β-strand | 408-411 | 4 | 2 |
| α-helix | 412-417 | 6 | |
| α-helix | 421-437 | 17 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Chain C: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 312-322 | 11 | |
| α-helix | 324-327 | 4 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-394 | 23 | |
| β-strand | 401-405 | 5 | 3 |
| β-strand | 408-411 | 4 | 3 |
| α-helix | 412-415 | 4 | |
| α-helix | 421-438 | 18 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Chain D: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 312-322 | 11 | |
| α-helix | 323-327 | 5 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-394 | 23 | |
| β-strand | 401-405 | 5 | 4 |
| β-strand | 408-411 | 4 | 4 |
| α-helix | 412-417 | 6 | |
| α-helix | 421-437 | 17 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Chain E: 13 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 307-309 | 3 | |
| α-helix | 312-322 | 11 | |
| α-helix | 324-327 | 4 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-395 | 24 | |
| β-strand | 401-405 | 5 | 5 |
| β-strand | 408-411 | 4 | 5 |
| α-helix | 412-417 | 6 | |
| α-helix | 421-438 | 18 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Chain F: 13 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 307-309 | 3 | |
| α-helix | 312-322 | 11 | |
| α-helix | 324-327 | 4 | |
| α-helix | 339-362 | 24 | |
| α-helix | 367-369 | 3 | |
| α-helix | 372-395 | 24 | |
| β-strand | 401-405 | 5 | 6 |
| β-strand | 408-411 | 4 | 6 |
| α-helix | 412-417 | 6 | |
| α-helix | 421-437 | 17 | |
| α-helix | 442-455 | 14 | |
| α-helix | 458-460 | 3 | |
| α-helix | 466-492 | 27 | |
| α-helix | 497-530 | 34 | |
| α-helix | 538-547 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Estrogen receptor | A, B, C, D, E, F | protein | 253 | Homo sapiens | P03372 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>1ERE_1 ESTROGEN RECEPTOR (chains A, B, C, D, E, F)
SKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINW
AKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEG
MVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLD
KITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLL
LEMLDAHRLHAPT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| EST | Estradiol | C18 H24 O2 | 6 |
Primary citation
Molecular basis of agonism and antagonism in the oestrogen receptor. Brzozowski, A.M., Pike, A.C., Dauter, Z. et al. Nature (1997) 389:753-758. DOI 10.1038/39645 · PubMed
Other PDB entries of the same protein (UniProt P03372 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7BAA 1.1 Å, Cys-42-tethered stabilizer 12 of 14-3-3(sigma)/ERa PPI
- 8BZC 1.1 Å, co-soaked stabilizers for ERa - 14-3-3 interaction (884_AZ244)
- 8BZW 1.1 Å, Co-soaked stabilizers for ERa - 14-3-3 interaction (844_AZ210)
- 8C04 1.1 Å, Co-soaked stabilizers for ERa - 14-3-3 interaction (884_AZ354)
- 7B9R 1.15 Å, Cys-45-tethered stabilizer 4 of 14-3-3(sigma)/ERa PPI
- 7B9T 1.15 Å, Cys-45-tethered stabilizer 5 of 14-3-3(sigma)/ERa PPI
- 7NFW 1.19 Å, Human 14-3-3 sigma in complex with human Estrogen Receptor alpha peptide
- 6HMU 1.2 Å, Ternary complex of Estrogen Receptor alpha peptide and 14-3-3 sigma C45 mutant bound to…
- 7BA8 1.2 Å, Cys-42-tethered stabilizer 10 of 14-3-3(sigma)/ERa PPI
- 8APS 1.2 Å, Small molecular stabilizer for ERalpha and 14-3-3 (1083744)
- 8BX3 1.2 Å, fragment-linked stabilizer for ERa - 14-3-3 interaction (1074372)
- 8BXI 1.2 Å, fragment-linked stabilizer for ERa - 14-3-3 interaction (1074361)
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