Research workbench
Crystal structure of the GLUR4 ligand-binding domain in complex with kainate
Analyse Crystal structure of the GLUR4 ligand-binding domain in complex with kainate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EN3
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 4,GLUTAMATE receptor
- UniProt
- P19493
- Ligands
- KAI
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate receptor 4,GLUTAMATE receptor | protein | 257 | 38% helix, 21% strand | P19493 |
Ligands and binding sites
- KAI · 3-(carboxymethyl)-4-isopropenylproline · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.66 | 0.83 | 39 | KAI |
| 2 | 63 | 0.29 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3EN3 · Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate · the same entry in another collection · chain A against A, TM-score 1.00
- P19493 · AlphaFold monomer V2.0 prediction for glutamate receptor 4 (P19493) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P19493
- Elsewhere: RCSB PDB 3EN3 · PDBe 3EN3 · UniProt P19493
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