Research workbench
Crystal structure of the GLUK2 K531A-T779G lbd dimer in complex with glutamate
Analyse Crystal structure of the GLUK2 K531A-T779G lbd dimer in complex with glutamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BDN
- Type
- protein
- Length
- 993 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor, ionotropic kainate 2
- UniProt
- P42260
- Ligands
- GLU, NA
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor, ionotropic kainate 2 | protein | 250 | 39% helix, 22% strand | P42260 |
| B | Glutamate receptor, ionotropic kainate 2 | protein | 253 | 38% helix, 22% strand | P42260 |
| C | Glutamate receptor, ionotropic kainate 2 | protein | 246 | 41% helix, 22% strand | P42260 |
| D | Glutamate receptor, ionotropic kainate 2 | protein | 244 | 40% helix, 22% strand | P42260 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1131 | 0.81 | 0.82 | 133 | empty |
| 2 | 893 | 0.78 | 0.81 | 90 | empty |
| 3 | 508 | 0.77 | 0.84 | 76 | empty |
| 4 | 56 | 0.70 | 0.97 | 19 | GLU |
| 5 | 56 | 0.69 | 0.97 | 17 | GLU |
Interfaces
6 interfaces between chains.
- C–D · 1069 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 1028 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 725 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 305 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 192 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4BDN · Crystal structure of the GluK2 K531A-T779G LBD dimer in complex with glutamate · the same entry in another collection · chain D against D, TM-score 1.00
- P42260 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 2 (P42260) · a predicted model of the same protein · chain C 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 P42260
- Elsewhere: RCSB PDB 4BDN · PDBe 4BDN · UniProt P42260
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