Research workbench
Crystal structure of acachbp in complex with hosieine
Analyse Crystal structure of acachbp in complex with hosieine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SGV
- Type
- protein
- Length
- 2,051 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble acetylcholine receptor
- UniProt
- Q8WSF8
- Ligands
- LDQ, NAG
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, I, J | Soluble acetylcholine receptor | protein | 205 | 9% helix, 53% strand | Q8WSF8 |
| H | Soluble acetylcholine receptor | protein | 206 | 9% helix, 53% strand | Q8WSF8 |
Ligands and binding sites
- LDQ · Hosieine · ligand · 10 copies · chains A, E, B, C, D, F, J, G, H, I
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, C, J, E
- ACT · Acetate ion · additive · chains 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 | 1134 | 0.72 | 0.76 | 119 | empty |
| 2 | 295 | 0.71 | 0.85 | 44 | LDQ |
| 3 | 373 | 0.71 | 0.83 | 50 | LDQ |
| 4 | 305 | 0.70 | 0.84 | 43 | LDQ |
| 5 | 769 | 0.70 | 0.76 | 88 | empty |
Interfaces
20 interfaces between chains.
- F–G · 1407 Ų buried · 19 hydrogen bonds · protein-protein
- H–I · 1404 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 1393 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1389 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1385 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 6SGV · Crystal structure of AcAChBP in complex with hosieine · 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 6SGV · PDBe 6SGV · UniProt Q8WSF8
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