MolNFT v1 · #15220 · protein
Crystal titration experiments (AMPA co-crystals soaked in 10 mm brw)
1MXV · Glutamate receptor 2: “Crystal titration experiments (AMPA co-crystals soaked in 10 mm brw)”. X-ray diffraction, 1 ligand (ZN), 9 pockets (best druggability 0.80). MolNFT v1 #15220 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1MXV
- Type
- protein
- Length
- 775 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 0.80
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glutamate receptor 2 | protein | 258 | 38% helix, 21% strand | P19491 |
| B | Glutamate receptor 2 | protein | 259 | 36% 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.80 | 0.85 | 99 | empty |
| 2 | 64 | 0.74 | 0.98 | 21 | empty |
| 3 | 60 | 0.70 | 0.97 | 20 | empty |
| 4 | 55 | 0.69 | 0.97 | 20 | empty |
| 5 | 315 | 0.65 | 0.80 | 38 | empty |
Interfaces
3 interfaces between chains.
- A–C · 880 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 328 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 31 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1MXV · crystal titration experiments (AMPA co-crystals soaked in 10 mM 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 1MXV · PDBe 1MXV · UniProt P19491
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