Research workbench
GLUA2-L483Y-A665C ligand-binding domain in complex with the antagonist dnqx
Analyse GLUA2-L483Y-A665C ligand-binding domain in complex with the antagonist dnqx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L17
- Type
- protein
- Length
- 1,034 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- DNQ, SO4
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Glutamate receptor 2 | protein | 259 | 36% helix, 20% strand | P19491 |
| C, G | Glutamate receptor 2 | protein | 258 | 36% helix, 21% strand | P19491 |
Ligands and binding sites
- DNQ · 6,7-dinitroquinoxaline-2,3-dione · ligand · 4 copies · chains A, C, E, G
- SO4 · Sulfate ion · ion · 3 copies · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1197 | 0.81 | 0.82 | 137 | DNQ |
| 2 | 363 | 0.64 | 0.79 | 36 | DNQ |
| 3 | 271 | 0.63 | 0.81 | 34 | empty |
| 4 | 286 | 0.59 | 0.78 | 34 | DNQ |
| 5 | 112 | 0.42 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 926 Ų buried · 9 hydrogen bonds · protein-protein
- A–E · 327 Ų buried · 0 hydrogen bonds · protein-protein
- E–G · 66 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4L17 · GluA2-L483Y-A665C ligand-binding domain in complex with the antagonist DNQX · the same entry in another collection · chain A against A, 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
- Every structure of UniProt P19491
- Elsewhere: RCSB PDB 4L17 · PDBe 4L17 · UniProt P19491
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