Research workbench
Cryo-EM structure of inactive MGLU7 homodimer
Analyse Cryo-EM structure of inactive MGLU7 homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EPC
- Type
- protein
- Length
- 1,564 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 3 of metabotropic glutamate receptor 7
- Pockets
- 17 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 41% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Isoform 3 of metabotropic glutamate receptor 7 | protein | 782 | 41% helix, 9% strand | — |
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 987 | 0.85 | 0.86 | 117 | empty |
| 2 | 953 | 0.84 | 0.85 | 120 | empty |
| 3 | 806 | 0.71 | 0.77 | 59 | empty |
| 4 | 446 | 0.66 | 0.79 | 49 | empty |
| 5 | 493 | 0.66 | 0.78 | 59 | empty |
Interfaces
1 interface between chains.
- A–B · 1248 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 disulfide (disulfide).
Compared structures
- 7EPC · Cryo-EM structure of inactive mGlu7 homodimer · the same entry in another collection · chain B against B, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7EPC · PDBe 7EPC
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