Research workbench
Crystal structure of aplysia californica achbp in complex with D-tubocurarine
Analyse Crystal structure of aplysia californica achbp in complex with D-tubocurarine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XYT
- Type
- protein
- Length
- 2,050 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble acetylcholine receptor
- UniProt
- Q8WSF8
- Ligands
- TC9
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Soluble acetylcholine receptor | protein | 205 | 8% helix, 50% strand | Q8WSF8 |
Ligands and binding sites
- TC9 · D-tubocurarine · ligand · 5 copies · chains B, C, G, D, E, F, H, I
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 | 777 | 0.76 | 0.81 | 63 | TC9 |
| 2 | 740 | 0.74 | 0.80 | 67 | TC9 |
| 3 | 630 | 0.69 | 0.78 | 70 | TC9 |
| 4 | 556 | 0.69 | 0.78 | 60 | empty |
| 5 | 582 | 0.68 | 0.77 | 55 | empty |
Interfaces
12 interfaces between chains.
- F–J · 1290 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 1289 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1287 Ų buried · 13 hydrogen bonds · protein-protein
- H–I · 1254 Ų buried · 16 hydrogen bonds · protein-protein
- F–G · 1246 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 2XYT · Crystal structure of Aplysia californica AChBP in complex with d- tubocurarine · 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 2XYT · PDBe 2XYT · UniProt Q8WSF8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.