MolNFT v1 · #151849 · protein
The glic pentameric ligand-gated ion channel 2.22 resolution
6HZW · Proton-gated ion channel: “The glic pentameric ligand-gated ion channel 2.22 resolution”. X-ray diffraction, 3 ligands (PLC, NA, CL), 20 pockets (best druggability 0.81). MolNFT v1 #151849 on GenesisL1: 3D structure, binding sites…
- PDB
- 6HZW
- Type
- protein
- Length
- 1,555 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proton-gated ion channel
- UniProt
- Q7NDN8
- Ligands
- PLC, NA, CL
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Proton-gated ion channel | protein | 311 | 36% helix, 35% strand | Q7NDN8 |
Ligands and binding sites
- PLC · Diundecyl phosphatidyl choline · ligand · 15 copies · chains A, E, B, C, D
- NA · Sodium ion · metal · 6 copies · chains A, B, C, D, E
- CL · Chloride ion · ion · 7 copies · chains A, B, C, D, E
- LMT · Dodecyl-beta-D-maltoside · additive · 11 copies · chains A, B, E, C, D
- ACT · Acetate ion · additive · 10 copies · chains A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.81 | 0.82 | 62 | LMT, NA |
| 2 | 381 | 0.71 | 0.83 | 40 | empty |
| 3 | 359 | 0.71 | 0.83 | 47 | empty |
| 4 | 389 | 0.71 | 0.82 | 49 | empty |
| 5 | 350 | 0.69 | 0.82 | 46 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2280 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 2270 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 2261 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 2250 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2247 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
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 Q7NDN8
- Elsewhere: RCSB PDB 6HZW · PDBe 6HZW · UniProt Q7NDN8
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