Research workbench
Crystal structure of the GluR2-flip ligand binding domain, r/g unedited.
Analyse Crystal structure of the GluR2-flip ligand binding domain, r/g unedited. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UXA
- Type
- protein
- Length
- 780 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.38
- Source
- RATTUS NORVEGICUS
- Molecule
- Glutamate receptor subunit GLUR2-flip
- UniProt
- Q9R174
- Ligands
- GLU, ZN
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.38 · 3 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor subunit GLUR2-flip | protein | 261 | 38% helix, 21% strand | Q9R174 |
| B | Glutamate receptor subunit GLUR2-flip | protein | 260 | 36% helix, 21% strand | Q9R174 |
| C | Glutamate receptor subunit GLUR2-flip | protein | 259 | 37% helix, 21% strand | Q9R174 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.78 | 0.83 | 96 | empty |
| 2 | 867 | 0.70 | 0.76 | 77 | empty |
| 3 | 91 | 0.56 | 0.86 | 25 | empty |
| 4 | 99 | 0.38 | 0.76 | 18 | empty |
| 5 | 122 | 0.38 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1030 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 282 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 84 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2UXA · Crystal structure of the GLUR2-flip ligand binding domain, R/G unedited. · 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 Q9R174
- Elsewhere: RCSB PDB 2UXA · PDBe 2UXA · UniProt Q9R174
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