Research workbench
Electron density MAP of GLUA2EM in complex with quisqualate and LY451646
Analyse Electron density MAP of GLUA2EM in complex with quisqualate and LY451646 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UQK
- Type
- protein
- Length
- 2,526 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- QUS
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 2 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Glutamate receptor 2 | protein | 631 | 35% helix, 22% strand | P19491 |
| B, C | Glutamate receptor 2 | protein | 632 | 35% helix, 22% strand | P19491 |
Ligands and binding sites
- QUS · (S)-2-amino-3-(3,5-dioxo-[1,2,4]oxadiazolidin-2-yl)-propionic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 691 | 0.75 | 0.81 | 89 | empty |
| 2 | 468 | 0.73 | 0.82 | 66 | empty |
| 3 | 491 | 0.70 | 0.80 | 53 | empty |
| 4 | 501 | 0.70 | 0.80 | 56 | empty |
| 5 | 478 | 0.70 | 0.80 | 53 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1370 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1367 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 963 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 961 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 175 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 4UQK · Electron density map of GluA2em in complex with quisqualate and LY451646 · 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 4UQK · PDBe 4UQK · UniProt P19491
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