Research workbench
Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with nms
Analyse Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZKC
- Type
- protein
- Length
- 384 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Muscarinic acetylcholine receptor M2,APO-cytochrome B562, muscarinic acetylcholine…
- UniProt
- P08172
- Ligands
- 3C0
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Muscarinic acetylcholine receptor M2,APO-cytochrome B562, muscarinic acetylcholine receptor M2 | protein | 384 | 82% 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
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.82 | 0.97 | 23 | 3C0 |
| 2 | 268 | 0.59 | 0.78 | 21 | empty |
| 3 | 129 | 0.59 | 0.84 | 24 | empty |
| 4 | 71 | 0.31 | 0.74 | 14 | empty |
| 5 | 54 | 0.24 | 0.72 | 12 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5ZKC · Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor… · 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 0.74
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 5ZKC · PDBe 5ZKC · UniProt P08172
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