Research workbench
Crystal structure of acetylcholine-binding protein (achbp) from aplysia californica in complex with hepes
Analyse Crystal structure of acetylcholine-binding protein (achbp) from aplysia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BR7
- Type
- protein
- Length
- 1,025 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble acetylcholine receptor
- UniProt
- Q8WSF8
- Pockets
- 17 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Soluble acetylcholine receptor | protein | 205 | 5% helix, 50% strand | Q8WSF8 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic 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
17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.69 | 0.81 | 57 | EPE |
| 2 | 408 | 0.69 | 0.81 | 58 | EPE |
| 3 | 391 | 0.69 | 0.81 | 53 | EPE |
| 4 | 371 | 0.68 | 0.81 | 53 | EPE |
| 5 | 428 | 0.63 | 0.77 | 47 | empty |
Interfaces
5 interfaces between chains.
- D–E · 1443 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1405 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1371 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1366 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 1216 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 2BR7 · Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in… · 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 2BR7 · PDBe 2BR7 · UniProt Q8WSF8
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