Research workbench
Crystal structure of the GLUR2 ligand binding core (S1S2J) in complex with AMPA at 1.7 resolution
Analyse Crystal structure of the GLUR2 ligand binding core (S1S2J) in complex with AMPA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FTM
- Type
- protein
- Length
- 774 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor subunit 2
- UniProt
- P19491
- Ligands
- AMQ, ZN
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate receptor subunit 2 | protein | 258 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- AMQ · (S)-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.77 | 0.84 | 92 | empty |
| 2 | 58 | 0.73 | 0.99 | 19 | AMQ |
| 3 | 53 | 0.71 | 0.98 | 20 | AMQ |
| 4 | 604 | 0.69 | 0.78 | 56 | empty |
| 5 | 262 | 0.57 | 0.78 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–C · 954 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 265 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 34 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1FTM · Crystal structure of the GLUR2 ligand binding core (S1S2J) in complex with AMPA at 1.7… · the same entry in another collection · chain B against B, 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 0.97
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 1FTM · PDBe 1FTM · UniProt P19491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.