MolNFT v1 · #99853 · protein
Crystal structure of hera-lbd (Y537S) in complex with chlordecone
4MG5 · Estrogen receptor: “Crystal structure of hera-lbd (Y537S) in complex with chlordecone”. X-ray diffraction, 1 ligand (27E), 8 pockets (best druggability 0.85). MolNFT v1 #99853 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4MG5
- 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 1
- UniProt
- P03372, Q15788
- Ligands
- 27E
- Pockets
- 8 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 241 | 69% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 236 | 68% helix, 4% strand | P03372 |
| C | Nuclear receptor coactivator 1 | protein | 9 | 78% helix, 0% strand | Q15788 |
| D | Nuclear receptor coactivator 1 | protein | 10 | 70% helix, 0% strand | Q15788 |
Ligands and binding sites
- 27E · Chlordecone · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 244 | 0.85 | 0.97 | 23 | 27E |
| 2 | 221 | 0.84 | 0.96 | 23 | 27E |
| 3 | 99 | 0.65 | 0.90 | 19 | empty |
| 4 | 88 | 0.62 | 0.89 | 17 | empty |
| 5 | 242 | 0.53 | 0.76 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1627 Ų buried · 24 hydrogen bonds · protein-protein
- B–D · 501 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 482 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
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 Q15788
- Elsewhere: RCSB PDB 4MG5 · PDBe 4MG5 · UniProt P03372 · UniProt Q15788
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