Research workbench
Crystal structure of achbp from bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors
Analyse Crystal structure of achbp from bulinus truncatus revals the conserved… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJ0
- Type
- protein
- Length
- 1,015 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine-binding protein
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Acetylcholine-binding protein | protein | 203 | 9% helix, 47% strand | — |
Ligands and binding sites
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 4 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.74 | 0.95 | 18 | CXS |
| 2 | 377 | 0.70 | 0.82 | 51 | CXS |
| 3 | 478 | 0.70 | 0.80 | 70 | CXS |
| 4 | 332 | 0.68 | 0.82 | 38 | CXS |
| 5 | 170 | 0.65 | 0.86 | 32 | empty |
Interfaces
5 interfaces between chains.
- A–E · 1540 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 1498 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1447 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1441 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1398 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 2BJ0 · Crystal Structure of AChBP from Bulinus truncatus revals the conserved structural… · 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
- Elsewhere: RCSB PDB 2BJ0 · PDBe 2BJ0
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