Research workbench
X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (S)-atpa at 1.9 a resolution. crystallization without zinc ions.
Analyse X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NNP
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- CE2, SO4
- Pockets
- 6 · 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 | Glutamate receptor 2 | protein | 258 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- CE2 · 3-(5-tert-butyl-3-oxidoisoxazol-4-yl)-L-alaninate · 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
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.77 | 0.81 | 98 | SO4 |
| 2 | 85 | 0.76 | 0.98 | 19 | CE2 |
| 3 | 71 | 0.75 | 0.98 | 19 | CE2 |
| 4 | 261 | 0.57 | 0.78 | 33 | empty |
| 5 | 79 | 0.38 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 943 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1NNP · X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.9… · 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 1NNP · PDBe 1NNP · UniProt P19491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.