Research workbench
X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (S)-thio-atpa at 2.2 a resolution.
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
- 2AIX
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- U1K
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 258 | 39% helix, 21% strand | P19491 |
Ligands and binding sites
- U1K · (S)-2-amino-3-(3-hydroxy-5-tert-butylisothiazol-4-yl) proprionic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.74 | 0.97 | 21 | U1K |
| 2 | 164 | 0.47 | 0.76 | 27 | empty |
| 3 | 95 | 0.37 | 0.75 | 24 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2AIX · X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (s)-thio-atpa at… · 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 2AIX · PDBe 2AIX · UniProt P19491
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