MolNFT v1 · #76468 · protein
Crystal structure of a GLUK2 (GLUR6) glycan wedge homodimer assembly
3QLT · Glutamate receptor, ionotropic kainate 2: “Crystal structure of a GLUK2 (GLUR6) glycan wedge homodimer assembly”. X-ray diffraction, 1 ligand (NAG), 8 pockets (best druggability 0.78). MolNFT v1 #76468 on GenesisL1: 3D structure…
- PDB
- 3QLT
- Type
- protein
- Length
- 738 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor, ionotropic kainate 2
- UniProt
- P42260
- Ligands
- NAG
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor, ionotropic kainate 2 | protein | 371 | 35% helix, 21% strand | P42260 |
| B | Glutamate receptor, ionotropic kainate 2 | protein | 367 | 36% helix, 22% strand | P42260 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 959 | 0.78 | 0.80 | 99 | empty |
| 2 | 806 | 0.73 | 0.78 | 77 | empty |
| 3 | 61 | 0.63 | 0.92 | 18 | empty |
| 4 | 188 | 0.47 | 0.76 | 22 | empty |
| 5 | 56 | 0.44 | 0.83 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1625 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 3QLT · Crystal structure of a GluK2 (GluR6) glycan wedge homodimer assembly · the same entry in another collection · chain B against B, 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 P42260
- Elsewhere: RCSB PDB 3QLT · PDBe 3QLT · UniProt P42260
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