Research workbench
Cryoem structure of full-length MGLU2 bound to ago-pam ADX55164 and glutamate
Analyse Cryoem structure of full-length MGLU2 bound to ago-pam ADX55164 and glutamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MTR
- Type
- protein
- Length
- 1,524 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metabotropic glutamate receptor 2
- UniProt
- Q14416
- Ligands
- GLU, ZQY, NAG
- Pockets
- 16 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Metabotropic glutamate receptor 2 | protein | 760 | 45% helix, 15% strand | Q14416 |
| A | Metabotropic glutamate receptor 2 | protein | 764 | 43% helix, 16% strand | Q14416 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 2 copies · chains B, A
- ZQY · 2-methoxy-6-propyl-N-(2-{4-[(1H-tetrazol-5-yl) methoxy]phenyl}ethyl)thieno[2,3-d]pyrimidin-4-amine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1126 | 0.82 | 0.83 | 128 | ZQY |
| 2 | 1056 | 0.79 | 0.81 | 106 | GLU |
| 3 | 915 | 0.78 | 0.80 | 90 | empty |
| 4 | 704 | 0.75 | 0.80 | 62 | empty |
| 5 | 507 | 0.74 | 0.82 | 70 | GLU |
Interfaces
1 interface between chains.
- B–A · 1297 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide, 2 glycan, 1 covalent (disulfide, N-glycosylation, covalent ligand).
Compared structures
- 7MTR · CryoEM Structure of Full-Length mGlu2 Bound to Ago-PAM ADX55164 and Glutamate · the same entry in another collection · chain A against A, TM-score 1.00
- Q14416 · AlphaFold monomer V2.0 prediction for metabotropic glutamate receptor 2 (Q14416) · a predicted model of the same protein · chain B against A, TM-score 0.86
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 7MTR · PDBe 7MTR · UniProt Q14416
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