MolNFT v1 · #14312 · protein
X-ray structure of the GLUR2 ligand binding core (S1S2J) in complex with 2-me-tet-AMPA at 1.85 a resolution.
1M5B · Glutamate receptor 2: “X-ray structure of the GLUR2 ligand binding core (S1S2J) in complex with 2-me-tet-AMPA at 1.85 a resolution.”. X-ray diffraction, 2 ligands (BN1, ZN), 8 pockets (best druggability 0.79). MolNFT v1 #14312 on…
- PDB
- 1M5B
- Type
- protein
- Length
- 774 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor 2
- UniProt
- P19491
- Ligands
- BN1, ZN
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate receptor 2 | protein | 258 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- BN1 · (S)-2-amino-3-[3-hydroxy-5-(2-methyl-2H-tetrazol-5-yl)isoxazol-4-yl]propionic acid · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 765 | 0.79 | 0.82 | 96 | empty |
| 2 | 72 | 0.74 | 0.98 | 21 | BN1 |
| 3 | 70 | 0.74 | 0.98 | 20 | BN1 |
| 4 | 268 | 0.73 | 0.87 | 45 | empty |
| 5 | 70 | 0.73 | 0.97 | 20 | BN1 |
Interfaces
3 interfaces between chains.
- A–C · 965 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 288 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 77 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1M5B · X-RAY STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH 2-Me-Tet-AMPA AT… · 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 1M5B · PDBe 1M5B · UniProt P19491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.