Research workbench
The structure and super-organization of acetylcholine receptor-rapsyn complexes
Analyse The structure and super-organization of acetylcholine receptor-rapsyn complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BOG
- Type
- protein
- Length
- 11,094 residues
- Chains
- 30
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholine receptor beta subunit; Acetylcholine receptor delta subunit; Acetylcholine…
- UniProt
- Q6S3I0, Q6S3H8, P02711, Q6S3H9
- Pockets
- 20 · best druggability 0.90
Structure
electron microscopy · 4 distinct chains · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0, B, G, L, Q, V | Acetylcholine receptor beta subunit | protein | 370 | 38% helix, 19% strand | Q6S3I0 |
| 1, C, H, M, R, W | Acetylcholine receptor delta subunit | protein | 369 | 42% helix, 22% strand | Q6S3H8 |
| 2, A, D, F, I, K, N, P, S, U, X, Z | Acetylcholine receptor subunit alpha | protein | 370 | 44% helix, 20% strand | P02711 |
| 3, E, J, O, T, Y | Acetylcholine receptor gamma subunit | protein | 370 | 42% helix, 18% strand | Q6S3H9 |
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 | 1032 | 0.90 | 0.91 | 144 | empty |
| 2 | 890 | 0.89 | 0.91 | 114 | empty |
| 3 | 818 | 0.88 | 0.91 | 115 | empty |
| 4 | 822 | 0.88 | 0.90 | 111 | empty |
| 5 | 766 | 0.88 | 0.91 | 111 | empty |
Interfaces
30 interfaces between chains.
- V–W · 1957 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1952 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 1949 Ų buried · 14 hydrogen bonds · protein-protein
- L–M · 1948 Ų buried · 14 hydrogen bonds · protein-protein
- Q–R · 1948 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 42 disulfide (disulfide).
Compared structures
- 4BOG · The structure and super-organization of acetylcholine receptor-rapsyn complexes · the same entry in another collection · chain I against I, 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 Q6S3I0
- Every structure of UniProt Q6S3H8
- Every structure of UniProt P02711
- Every structure of UniProt Q6S3H9
- Elsewhere: RCSB PDB 4BOG · PDBe 4BOG · UniProt Q6S3I0 · UniProt Q6S3H8 · UniProt P02711 · UniProt Q6S3H9
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