Research workbench
Activated GLUA2 complex bound to glutamate, cyclothiazide, and stz in digitonin
Analyse Activated GLUA2 complex bound to glutamate, cyclothiazide, and stz in digitonin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WEO
- Type
- protein
- Length
- 3,950 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit chimera
- UniProt
- P19491, O88602
- Ligands
- GLU, CYZ
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit chimera | protein | 988 | 43% helix, 15% strand | P19491, O88602 |
| B, D | Glutamate receptor 2,VOLTAGE-dependent calcium channel gamma-2 subunit chimera | protein | 987 | 42% helix, 15% strand | P19491, O88602 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 4 copies · chains A, B, C, D
- CYZ · Cyclothiazide · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.87 | 0.87 | 139 | empty |
| 2 | 967 | 0.82 | 0.84 | 103 | CYZ |
| 3 | 1000 | 0.82 | 0.83 | 106 | CYZ |
| 4 | 131 | 0.80 | 0.97 | 37 | empty |
| 5 | 860 | 0.80 | 0.82 | 93 | empty |
Interfaces
5 interfaces between chains.
- C–D · 3873 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 3845 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 3124 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 3046 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 343 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 5WEO · Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin · the same entry in another collection · chain C against C, 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 0.71
- O88602 · AlphaFold monomer V2.0 prediction for voltage-dependent calcium channel gamma-2 subunit… · a predicted model of the same protein · chain D against A, TM-score 0.19
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
- Every structure of UniProt O88602
- Elsewhere: RCSB PDB 5WEO · PDBe 5WEO · UniProt P19491 · UniProt O88602
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