MolNFT v1 · #53195 · protein
Crystal structure of aplysia achbp in complex with tropisetron
2WNC · Soluble acetylcholine receptor: “Crystal structure of aplysia achbp in complex with tropisetron”. X-ray diffraction, 1 ligand (TKT), 20 pockets (best druggability 0.72). MolNFT v1 #53195 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2WNC
- Type
- protein
- Length
- 1,066 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble acetylcholine receptor
- UniProt
- Q8WSF8
- Ligands
- TKT
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble acetylcholine receptor | protein | 215 | 12% helix, 48% strand | Q8WSF8 |
| B, E | Soluble acetylcholine receptor | protein | 213 | 12% helix, 48% strand | Q8WSF8 |
| C | Soluble acetylcholine receptor | protein | 212 | 11% helix, 50% strand | Q8WSF8 |
| D | Soluble acetylcholine receptor | protein | 213 | 11% helix, 49% strand | Q8WSF8 |
Ligands and binding sites
- TKT · (3-endo)-8-methyl-8-azabicyclo[3.2.1]oct-3-yl 1H-indole-3-carboxylate · ligand · 5 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, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 606 | 0.72 | 0.79 | 73 | TKT |
| 2 | 499 | 0.69 | 0.79 | 59 | TKT |
| 3 | 485 | 0.68 | 0.79 | 57 | TKT |
| 4 | 470 | 0.68 | 0.79 | 58 | TKT |
| 5 | 321 | 0.64 | 0.80 | 40 | TKT |
Interfaces
5 interfaces between chains.
- A–B · 1452 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 1395 Ų buried · 16 hydrogen bonds · protein-protein
- A–E · 1394 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1381 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1372 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 2WNC · Crystal structure of Aplysia ACHBP in complex with tropisetron · 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 Q8WSF8
- Elsewhere: RCSB PDB 2WNC · PDBe 2WNC · UniProt Q8WSF8
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