Research workbench
Er-prs*(-) (L536S, L372R) in complex with raloxifene
Analyse Er-prs*(-) (L536S, L372R) in complex with raloxifene in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NDO
- Type
- protein
- Length
- 469 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor
- UniProt
- P03372
- Ligands
- RAL, CL
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 232 | 68% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 237 | 70% helix, 4% strand | P03372 |
Ligands and binding sites
- RAL · Raloxifene · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.82 | 0.92 | 32 | RAL |
| 2 | 315 | 0.80 | 0.90 | 31 | RAL |
| 3 | 320 | 0.70 | 0.84 | 39 | empty |
| 4 | 100 | 0.65 | 0.90 | 18 | EDO |
| 5 | 96 | 0.63 | 0.89 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1804 Ų buried · 26 hydrogen bonds · protein-protein
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 7NDO · PDBe 7NDO · UniProt P03372
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