Research workbench
mGluR3 complexed with glutamate analog
Analyse mGluR3 complexed with glutamate analog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CNM
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.84
- Source
- Homo sapiens
- Molecule
- Metabotropic glutamate receptor 3
- UniProt
- Q14832
- Ligands
- 52Q, MG, CL, SO4
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · resolution 2.84 · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metabotropic glutamate receptor 3 | protein | 434 | 39% helix, 20% strand | Q14832 |
Ligands and binding sites
- 52Q · (1R,2S,4R,5R,6R)-2-amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-2,6-dicarboxylic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.58 | 0.84 | 27 | empty |
| 2 | 286 | 0.55 | 0.76 | 33 | 52Q, CL |
| 3 | 66 | 0.35 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 3 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 Q14832
- Elsewhere: RCSB PDB 5CNM · PDBe 5CNM · UniProt Q14832
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