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Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y- N754S) in complex with glutamate and me-CX516 at 1.72 a resolution
Analyse Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y- N754S) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IY6
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- MQS, MQR, GLU, SO4
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 263 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- MQS · [(3S)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone · ligand · 2 copies · chains A
- MQR · [(3R)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone · ligand · chains A
- GLU · Glutamic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.43 | 0.76 | 24 | SO4 |
| 2 | 62 | 0.35 | 0.77 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4IY6 · Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with… · 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 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 4IY6 · PDBe 4IY6 · UniProt P19491
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