Research workbench
Crystal structure of rat glutamate receptor delta-2 extracellular domain
Analyse Crystal structure of rat glutamate receptor delta-2 extracellular domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L2E
- Type
- protein
- Length
- 1,944 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor ionotropic, delta-2,GLUTAMATE receptor ionotropic, delta-2
- UniProt
- Q63226
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate receptor ionotropic, delta-2,GLUTAMATE receptor ionotropic, delta-2 | protein | 648 | 38% helix, 22% strand | Q63226 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 801 | 0.78 | 0.82 | 88 | empty |
| 2 | 397 | 0.67 | 0.80 | 39 | empty |
| 3 | 413 | 0.66 | 0.79 | 35 | empty |
| 4 | 310 | 0.65 | 0.81 | 25 | empty |
| 5 | 373 | 0.63 | 0.78 | 41 | empty |
Interfaces
1 interface between chains.
- B–C · 2016 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 5L2E · Crystal structure of rat Glutamate receptor delta-2 extracellular domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q63226 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, delta-2 (Q63226) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 Q63226
- Elsewhere: RCSB PDB 5L2E · PDBe 5L2E · UniProt Q63226
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