Research workbench
Kainate bound to the D655A mutant of the ligand binding domain of GLUA3
Analyse Kainate bound to the D655A mutant of the ligand binding domain of GLUA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F31
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 3
- UniProt
- P19492
- Ligands
- KAI, ZN
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, D | Glutamate receptor 3 | protein | 258 | 38% helix, 20% strand | P19492 |
Ligands and binding sites
- KAI · 3-(carboxymethyl)-4-isopropenylproline · ligand · 2 copies · chains B, D
- ZN · Zinc ion · metal · 4 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1171 | 0.79 | 0.81 | 112 | KAI |
| 2 | 158 | 0.64 | 0.86 | 30 | KAI |
| 3 | 222 | 0.64 | 0.83 | 30 | empty |
Interfaces
1 interface between chains.
- B–D · 765 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4F31 · Kainate bound to the D655A mutant of the ligand binding domain of GluA3 · the same entry in another collection · chain D against D, TM-score 1.00
- P19492 · AlphaFold monomer V2.0 prediction for glutamate receptor 3 (P19492) · a predicted model of the same protein · chain B 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 P19492
- Elsewhere: RCSB PDB 4F31 · PDBe 4F31 · UniProt P19492
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