Research workbench
GLUA2(FLOP) S729C ligand binding core dimer bound to nbqx at 1.76 ångström resolution
Analyse GLUA2(FLOP) S729C ligand binding core dimer bound to nbqx at 1.76 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FQH
- Type
- protein
- Length
- 517 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2,GLUTAMATE receptor 2
- UniProt
- P19491
- Ligands
- E2Q
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2,GLUTAMATE receptor 2 | protein | 259 | 38% helix, 21% strand | P19491 |
| B | Glutamate receptor 2,GLUTAMATE receptor 2 | protein | 258 | 38% helix, 23% strand | P19491 |
Ligands and binding sites
- E2Q · 6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.75 | 0.92 | 26 | empty |
| 2 | 987 | 0.74 | 0.77 | 78 | empty |
| 3 | 212 | 0.60 | 0.81 | 41 | empty |
| 4 | 228 | 0.53 | 0.77 | 30 | E2Q |
| 5 | 159 | 0.53 | 0.80 | 21 | E2Q |
Interfaces
1 interface between chains.
- A–B · 977 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6FQH · GluA2(flop) S729C ligand binding core dimer bound to NBQX at 1.76 Angstrom resolution · 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 6FQH · PDBe 6FQH · UniProt P19491
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