Research workbench
Ligand-binding domain of GLUA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
Analyse Ligand-binding domain of GLUA2 (flip) ionotropic glutamate receptor in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PMW
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- GLU, G69, SO4
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 261 | 36% helix, 21% strand | P19491 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
- G69 · N-[(2S)-5-{[4-(hydroxymethyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl}-2,3-dihydro-1H-inden-2-yl]propane-2-sulfonami de · ligand · chains A
- SO4 · Sulfate ion · ion · 7 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- DMS · Dimethyl sulfoxide · 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 | 136 | 0.47 | 0.78 | 26 | SO4 |
| 2 | 125 | 0.42 | 0.76 | 26 | SO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3PMW · Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an… · 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 3PMW · PDBe 3PMW · UniProt P19491
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