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GLUA2(FLOP) G724C ligand binding core dimer bound to L-glutamate (form B) at 2.91 ångström resolution
Analyse GLUA2(FLOP) G724C ligand binding core dimer bound to L-glutamate (form B) at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FQI
- Type
- protein
- Length
- 520 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
- GGL
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2,GLUTAMATE receptor 2 | protein | 259 | 38% helix, 22% strand | P19491 |
| B | Glutamate receptor 2,GLUTAMATE receptor 2 | protein | 261 | 39% helix, 20% strand | P19491 |
Ligands and binding sites
- GGL · Gamma-L-glutamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 830 | 0.73 | 0.78 | 78 | empty |
| 2 | 104 | 0.43 | 0.78 | 20 | empty |
| 3 | 88 | 0.39 | 0.77 | 27 | empty |
| 4 | 74 | 0.37 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 486 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6FQI · GluA2(flop) G724C ligand binding core dimer bound to L-Glutamate (Form B) at 2.91… · the same entry in another collection · chain A against A, TM-score 1.00
- P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 6FQI · PDBe 6FQI · UniProt P19491
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