Research workbench
Cryo-EM structure of a class a GPCR-G protein complex
Analyse Cryo-EM structure of a class a GPCR-G protein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V69
- Type
- protein
- Length
- 1,122 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I) subunit alpha-1; Guanine nucleotide-binding…
- UniProt
- P63096, P62873, P59768, P08173
- Pockets
- 14 · best druggability 0.81
Structure
electron microscopy · 5 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(I) subunit alpha-1 | protein | 218 | 46% helix, 15% strand | P63096 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 338 | 8% helix, 41% strand | P62873 |
| C | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 57 | 46% helix, 0% strand | P59768 |
| S | SCFV16 | protein | 232 | 4% helix, 40% strand | — |
| R | Muscarinic acetylcholine receptor M4 | protein | 277 | 79% helix, 0% strand | P08173 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.81 | 0.86 | 60 | empty |
| 2 | 87 | 0.77 | 0.98 | 19 | empty |
| 3 | 1167 | 0.71 | 0.75 | 109 | empty |
| 4 | 216 | 0.62 | 0.81 | 29 | empty |
| 5 | 176 | 0.56 | 0.80 | 26 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2198 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1157 Ų buried · 12 hydrogen bonds · protein-protein
- A–R · 900 Ų buried · 9 hydrogen bonds · protein-protein
- A–S · 587 Ų buried · 11 hydrogen bonds · protein-protein
- B–S · 429 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7V69 · Cryo-EM structure of a class A GPCR-G protein complex · the same entry in another collection · chain R against R, TM-score 1.00
- 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 B against A, TM-score 0.99
- P08173 · AlphaFold monomer V2.0 prediction for muscarinic acetylcholine receptor M4 (P08173) · a predicted model of the same protein · chain R against A, TM-score 0.93
- 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 C against A, TM-score 0.90
- P63096 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P63096
- Every structure of UniProt P62873
- Every structure of UniProt P59768
- Every structure of UniProt P08173
- Elsewhere: RCSB PDB 7V69 · PDBe 7V69 · UniProt P63096 · UniProt P62873 · UniProt P59768 · UniProt P08173
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