MolNFT v1 · #15226 · protein
Crystal titration experiments (AMPA co-crystals soaked in 10 nm brw)
1MY1 · Glutamate receptor 2: “Crystal titration experiments (AMPA co-crystals soaked in 10 nm brw)”. X-ray diffraction, 1 ligand (ZN), 9 pockets (best druggability 0.79). MolNFT v1 #15226 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1MY1
- 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
- ZN
- Pockets
- 9 · 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
- 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
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1197 | 0.79 | 0.81 | 140 | empty |
| 2 | 61 | 0.73 | 0.99 | 21 | empty |
| 3 | 57 | 0.73 | 0.99 | 21 | empty |
| 4 | 53 | 0.71 | 0.98 | 19 | empty |
| 5 | 256 | 0.56 | 0.78 | 30 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1016 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 273 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 104 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1MY1 · crystal titration experiments (AMPA co-crystals soaked in 10 nM BrW) · 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 1MY1 · PDBe 1MY1 · UniProt P19491
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