MolNFT v1 · #177654 · protein
Cryo-EM structure of inactive MGLU2 homodimer
7EPA · Metabotropic glutamate receptor 2: “Cryo-EM structure of inactive MGLU2 homodimer”. Electron microscopy, 18 pockets (best druggability 0.83). MolNFT v1 #177654 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7EPA
- Type
- protein
- Length
- 1,564 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metabotropic glutamate receptor 2
- UniProt
- Q14416
- Pockets
- 18 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 43% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Metabotropic glutamate receptor 2 | protein | 782 | 43% helix, 11% strand | Q14416 |
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1083 | 0.83 | 0.84 | 124 | empty |
| 2 | 708 | 0.82 | 0.86 | 98 | empty |
| 3 | 988 | 0.75 | 0.78 | 87 | empty |
| 4 | 78 | 0.72 | 0.96 | 19 | empty |
| 5 | 764 | 0.71 | 0.77 | 87 | empty |
Interfaces
1 interface between chains.
- A–B · 1270 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 disulfide (disulfide).
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 Q14416
- Elsewhere: RCSB PDB 7EPA · PDBe 7EPA · UniProt Q14416
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