Research workbench
Crystal structure of the GLUR6 ligand binding core in complex with kainate 1.93 a resolution
Analyse Crystal structure of the GLUR6 ligand binding core in complex with kainate 1.93… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TT1
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor, ionotropic kainate 2
- UniProt
- P42260
- Ligands
- KAI
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutamate receptor, ionotropic kainate 2 | protein | 251 | 40% helix, 22% strand | P42260 |
Ligands and binding sites
- KAI · 3-(carboxymethyl)-4-isopropenylproline · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.77 | 0.79 | 73 | empty |
| 2 | 187 | 0.69 | 0.87 | 32 | KAI |
| 3 | 169 | 0.66 | 0.86 | 31 | KAI |
| 4 | 388 | 0.58 | 0.75 | 44 | empty |
| 5 | 333 | 0.57 | 0.76 | 48 | empty |
Interfaces
1 interface between chains.
- A–B · 772 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1TT1 · Crystal structure of the GLUR6 ligand binding core in complex with kainate 1.93 a… · the same entry in another collection · chain B against B, 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 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 P42260
- Elsewhere: RCSB PDB 1TT1 · PDBe 1TT1 · UniProt P42260
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