Research workbench
Crystal structure of M2 muscarinic acetylcholine receptor bound with nms
Analyse Crystal structure of M2 muscarinic acetylcholine receptor bound with nms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZK8
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Muscarinic acetylcholine receptor M2,REDESIGNED apo- cytochrome B562,MUSCARINIC…
- UniProt
- P08172
- Ligands
- 3C0
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Muscarinic acetylcholine receptor M2,REDESIGNED apo- cytochrome B562,MUSCARINIC acetylcholine receptor M2 | protein | 369 | 84% helix, 0% strand | P08172 |
Ligands and binding sites
- 3C0 · N-methyl scopolamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.83 | 0.96 | 31 | 3C0 |
| 2 | 280 | 0.60 | 0.78 | 21 | empty |
| 3 | 90 | 0.54 | 0.85 | 21 | empty |
| 4 | 85 | 0.34 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5ZK8 · Crystal structure of M2 muscarinic acetylcholine receptor bound with NMS · the same entry in another collection · chain A against A, TM-score 1.00
- P08172 · AlphaFold monomer V2.0 prediction for muscarinic acetylcholine receptor M2 (P08172) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P08172
- Elsewhere: RCSB PDB 5ZK8 · PDBe 5ZK8 · UniProt P08172
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