MolNFT v1 · #15041 · protein
X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (S)-des-me-AMPA at 1.97 a resolution, crystallization in the presence of zinc acetate
1MS7 · Glutamate receptor subunit 2: “X-ray structure of the GLUR2 ligand-binding core (S1S2J) in complex with (S)-des-me-AMPA at 1.97 a…”. X-ray diffraction, 2 ligands (SHI, ZN), 8 pockets (best druggability 0.76). MolNFT v1 #15041 on…
- PDB
- 1MS7
- Type
- protein
- Length
- 774 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate receptor subunit 2
- UniProt
- P19491
- Ligands
- SHI, ZN
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate receptor subunit 2 | protein | 258 | 38% helix, 21% strand | P19491 |
Ligands and binding sites
- SHI · (S)-2-amino-3-(3-hydroxy-isoxazol-4-yl)propionic acid · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 716 | 0.76 | 0.81 | 93 | empty |
| 2 | 52 | 0.71 | 0.99 | 19 | SHI |
| 3 | 275 | 0.57 | 0.78 | 28 | empty |
| 4 | 206 | 0.52 | 0.78 | 27 | empty |
| 5 | 69 | 0.46 | 0.83 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–C · 993 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 310 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1MS7 · X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA… · 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 1MS7 · PDBe 1MS7 · UniProt P19491
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