Research workbench
Quisqualate bound to the D655A mutant of the ligand binding domain of GLUA3
Analyse Quisqualate bound to the D655A mutant of the ligand binding domain of GLUA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F2Q
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 3
- UniProt
- P19492
- Ligands
- QUS, ZN
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 3 | protein | 258 | 38% helix, 22% strand | P19492 |
Ligands and binding sites
- QUS · (S)-2-amino-3-(3,5-dioxo-[1,2,4]oxadiazolidin-2-yl)-propionic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.40 | 0.76 | 27 | empty |
| 2 | 113 | 0.40 | 0.76 | 22 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4F2Q · Quisqualate bound to the D655A mutant of the ligand binding domain of GluA3 · the same entry in another collection · chain A against A, TM-score 1.00
- P19492 · AlphaFold monomer V2.0 prediction for glutamate receptor 3 (P19492) · 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 P19492
- Elsewhere: RCSB PDB 4F2Q · PDBe 4F2Q · UniProt P19492
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