MolNFT v1 · #17713 · protein
Crystal structure of the GLUR2 ligand-binding core (S1S2J) with the L483Y and L650T mutations and in complex with AMPA
1P1W · Glutamate receptor 2 precursor: “Crystal structure of the GLUR2 ligand-binding core (S1S2J) with the L483Y and L650T mutations and in complex…”. X-ray diffraction, 2 ligands (AMQ, SO4), 4 pockets (best druggability 0.76). MolNFT v1…
- PDB
- 1P1W
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2 precursor
- UniProt
- P19491
- Ligands
- AMQ, SO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutamate receptor 2 precursor | protein | 258 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- AMQ · (S)-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 723 | 0.76 | 0.81 | 105 | SO4 |
| 2 | 73 | 0.74 | 0.98 | 22 | AMQ |
| 3 | 64 | 0.71 | 0.97 | 22 | AMQ |
| 4 | 244 | 0.56 | 0.79 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 978 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1P1W · Crystal structure of the GluR2 ligand-binding core (S1S2J) with the L483Y and L650T… · the same entry in another collection · chain A against A, TM-score 1.00
- P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain B 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 1P1W · PDBe 1P1W · UniProt P19491
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