Research workbench
Cryo-EM structure of S1 state ACh-bound M2R-Go signaling complex with a PAM
Analyse Cryo-EM structure of S1 state ACh-bound M2R-Go signaling complex with a PAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T94
- Type
- protein
- Length
- 1,113 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.16
- Source
- Homo sapiens; Mus musculus
- Molecule
- Muscarinic acetylcholine receptor M2,muscarinic acetylcholine receptor M2 chimera…
- UniProt
- P08172, P09471, P62873, P59768
- Ligands
- ACH, 2CU
- Pockets
- 10 · best druggability 0.82
Structure
electron microscopy · resolution 3.16 · 5 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Muscarinic acetylcholine receptor M2,muscarinic acetylcholine receptor M2 chimera | protein | 265 | 77% helix, 0% strand | P08172 |
| B | Guanine nucleotide-binding protein G(o) subunit alpha | protein | 218 | 42% helix, 17% strand | P09471 |
| C | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 338 | 7% helix, 46% strand | P62873 |
| D | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 56 | 57% helix, 0% strand | P59768 |
| E | Antibody fragment | protein | 236 | 5% helix, 44% strand | — |
Ligands and binding sites
- ACH · Acetylcholine · ligand · chains A
- 2CU · 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1009 | 0.82 | 0.83 | 79 | empty |
| 2 | 432 | 0.77 | 0.85 | 51 | ACH, 2CU |
| 3 | 677 | 0.71 | 0.78 | 69 | empty |
| 4 | 447 | 0.67 | 0.79 | 53 | empty |
| 5 | 158 | 0.59 | 0.83 | 31 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2096 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1084 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 973 Ų buried · 5 hydrogen bonds · protein-protein
- B–E · 524 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 396 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain C against A, TM-score 0.99
- 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 0.92
- P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain D against A, TM-score 0.87
- P09471 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(O) subunit… · a predicted model of the same protein · chain B against A, TM-score 0.77
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
- Every structure of UniProt P09471
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Elsewhere: RCSB PDB 7T94 · PDBe 7T94 · UniProt P08172 · UniProt P09471 · UniProt P62873 · UniProt P59768
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