Research workbench
Crystal structure of the GLUR2 ligand binding core (S1S2J) in complex with quisqualate in a non zinc crystal form at 2.15 ångströms resolution
Analyse Crystal 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
- 1MM6
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- QUS, SO4
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 2 | protein | 261 | 36% helix, 21% strand | P19491 |
| B | Glutamate receptor 2 | protein | 259 | 37% helix, 21% strand | P19491 |
Ligands and binding sites
- QUS · (S)-2-amino-3-(3,5-dioxo-[1,2,4]oxadiazolidin-2-yl)-propionic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.74 | 0.81 | 75 | empty |
| 2 | 211 | 0.60 | 0.81 | 35 | SO4 |
| 3 | 286 | 0.59 | 0.79 | 32 | empty |
| 4 | 77 | 0.36 | 0.76 | 24 | empty |
| 5 | 54 | 0.27 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 895 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1MM6 · crystal structure of the GluR2 ligand binding core (S1S2J) in complex with quisqualate in… · 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 1MM6 · PDBe 1MM6 · UniProt P19491
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