Research workbench
Three-dimensional structure of the pentameric helical bundle of the acetylcholine receptor M2 transmembrane segment
Analyse Three-dimensional structure of the pentameric helical bundle of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EQ8
- Type
- protein
- Length
- 115 residues
- Chains
- 5
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine receptor protein
- UniProt
- P02718
- Ligands
- OH
- Pockets
- 1 · best druggability 0.79
Structure
solid-state nmr · 1 distinct chain · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Acetylcholine receptor protein | protein | 23 | 91% helix, 0% strand | P02718 |
Ligands and binding sites
- OH · Hydroxide ion · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1080 | 0.79 | 0.80 | 74 | empty |
Interfaces
5 interfaces between chains.
- A–B · 354 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 352 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 352 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 348 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 325 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1EQ8 · Three-dimensional structure of the pentameric helical bundle of the acetylcholine… · the same entry in another collection · chain D against D, TM-score 1.00
- P02718 · AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit delta (P02718) · a predicted model of the same protein · chain E against A, TM-score 0.70
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 P02718
- Elsewhere: RCSB PDB 1EQ8 · PDBe 1EQ8 · UniProt P02718
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