MolNFT v1 · #141072 · protein
Crystal structure of human P2X3 receptor in complex with the af-219 negative allosteric modulator
5YVE · P2X purinoceptor 3: “Crystal structure of human P2X3 receptor in complex with the af-219 negative allosteric modulator”. X-ray diffraction, 4 ligands (AF9, NAG, MG), 1 pocket (best druggability 0.31). MolNFT v1 #141072 on GenesisL1…
- PDB
- 5YVE
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P2X purinoceptor 3
- UniProt
- P56373
- Ligands
- AF9, NAG, MG, NA
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P2X purinoceptor 3 | protein | 327 | 27% helix, 39% strand | P56373 |
Ligands and binding sites
- AF9 · 5-[2,4-bis(azanyl)pyrimidin-5-yl]oxy-2-methoxy-4-propan-2-yl-benzenesulfonamide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.31 | 0.74 | 17 | MG |
Modifications
Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 5YVE · Crystal structure of human P2X3 receptor in complex with the AF-219 negative allosteric… · the same entry in another collection · chain A against A, TM-score 1.00
- P56373 · AlphaFold monomer V2.0 prediction for P2X purinoceptor 3 (P56373) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P56373
- Elsewhere: RCSB PDB 5YVE · PDBe 5YVE · UniProt P56373
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