Research workbench
AMPA subtype ionotropic glutamate receptor GLUA2 in complex with gyki- br
Analyse AMPA subtype ionotropic glutamate receptor GLUA2 in complex with gyki- br in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L1G
- Type
- protein
- Length
- 3,101 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- GYB, NAG
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Glutamate receptor 2 | protein | 777 | 39% helix, 18% strand | P19491 |
| B | Glutamate receptor 2 | protein | 773 | 38% helix, 18% strand | P19491 |
| C | Glutamate receptor 2 | protein | 774 | 39% helix, 18% strand | P19491 |
Ligands and binding sites
- GYB · (8R)-5-(4-amino-3-bromophenyl)-N,8-dimethyl-8,9-dihydro-2H,7H-[1,3]dioxolo[4,5-h][2,3]benzodiazepine-7-carboxamide · ligand · 5 copies · chains A, D, B, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1003 | 0.85 | 0.86 | 101 | empty |
| 2 | 851 | 0.81 | 0.83 | 98 | empty |
| 3 | 818 | 0.81 | 0.83 | 66 | GYB |
| 4 | 437 | 0.73 | 0.83 | 70 | empty |
| 5 | 435 | 0.71 | 0.82 | 54 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3623 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 3317 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 2945 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 2922 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 400 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 5 glycan, 1 covalent (disulfide, N-glycosylation, covalent ligand, glycation).
Compared structures
- 5L1G · AMPA subtype ionotropic glutamate receptor GluA2 in complex with GYKI-Br · the same entry in another collection · chain A against A, 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 P19491
- Elsewhere: RCSB PDB 5L1G · PDBe 5L1G · UniProt P19491
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