Research workbench
Human estrogen receptor alpha ligand-binding domain in complex with 2- (but-1-enyl)-17BETA-estradiol and a glucocorticoid receptor interacting protein 1 nr box II peptide
Analyse Human estrogen receptor alpha ligand-binding domain in complex with 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G5O
- Type
- protein
- Length
- 496 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Nuclear receptor coactivator 2
- UniProt
- P03372, Q15596
- Ligands
- DRQ
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 238 | 69% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 239 | 67% helix, 4% strand | P03372 |
| C | Nuclear receptor coactivator 2 | protein | 10 | 70% helix, 0% strand | Q15596 |
| D | Nuclear receptor coactivator 2 | protein | 9 | 56% helix, 0% strand | Q15596 |
Ligands and binding sites
- DRQ · (9alpha,13beta,17beta)-2-[(1Z)-but-1-en-1-yl]estra-1,3,5(10)-triene-3,17-diol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.84 | 0.97 | 23 | DRQ |
| 2 | 180 | 0.84 | 0.97 | 21 | DRQ |
| 3 | 540 | 0.66 | 0.77 | 50 | empty |
| 4 | 92 | 0.61 | 0.88 | 25 | empty |
| 5 | 93 | 0.59 | 0.87 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1804 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 512 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 499 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (artifact).
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 Q15596
- Elsewhere: RCSB PDB 2G5O · PDBe 2G5O · UniProt P03372 · UniProt Q15596
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