Research workbench
Structure of the complex of AMPA receptor GLUA2 with auxiliary subunit tarp gamma-5 bound to agonist glutamate
Analyse Structure of the complex of AMPA receptor GLUA2 with auxiliary subunit tarp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RZ6
- Type
- protein
- Length
- 3,534 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- GLU, PCW
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor 2 | protein | 983 | 46% helix, 16% strand | P19491 |
| B, D | Glutamate receptor 2 | protein | 784 | 40% helix, 13% strand | P19491 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 4 copies · chains A, B, C, D
- PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A, 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 | 1017 | 0.82 | 0.83 | 102 | empty |
| 2 | 357 | 0.81 | 0.91 | 54 | empty |
| 3 | 992 | 0.78 | 0.80 | 87 | empty |
| 4 | 804 | 0.78 | 0.82 | 79 | empty |
| 5 | 1006 | 0.78 | 0.80 | 84 | empty |
Interfaces
6 interfaces between chains.
- A–B · 4185 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 4083 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 2679 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 2553 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 407 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 7RZ6 · Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound… · the same entry in another collection · chain D against D, 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 0.68
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 7RZ6 · PDBe 7RZ6 · UniProt P19491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.