Research workbench
Cryo-EM structure of the partial agonist salbutamol-bound BETA2 adrenergic receptor-gs protein complex.
Analyse Cryo-EM structure of the partial agonist salbutamol-bound BETA2 adrenergic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DHI
- Type
- protein
- Length
- 1,019 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(S) subunit alpha isoforms short; Guanine…
- UniProt
- P63092, P62871, P63212, P07550
- Ligands
- 68H
- Pockets
- 13 · best druggability 0.82
Structure
electron microscopy · 5 distinct chains · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 216 | 42% helix, 17% strand | P63092 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 335 | 8% helix, 39% strand | P62871 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 52 | 50% helix, 0% strand | P63212 |
| N | NB35 nanobody | protein | 126 | 7% helix, 41% strand | — |
| R | Beta-2 adrenergic receptor | protein | 290 | 62% helix, 1% strand | P07550 |
Ligands and binding sites
- 68H · Salbutamol · ligand · chains R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 737 | 0.82 | 0.86 | 58 | empty |
| 2 | 396 | 0.77 | 0.86 | 43 | 68H |
| 3 | 945 | 0.76 | 0.79 | 73 | empty |
| 4 | 684 | 0.72 | 0.78 | 75 | empty |
| 5 | 663 | 0.68 | 0.77 | 59 | empty |
Interfaces
6 interfaces between chains.
- B–G · 1957 Ų buried · 13 hydrogen bonds · protein-protein
- A–R · 1532 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1389 Ų buried · 21 hydrogen bonds · protein-protein
- A–N · 809 Ų buried · 5 hydrogen bonds · protein-protein
- B–N · 478 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7DHI · Cryo-EM structure of the partial agonist salbutamol-bound beta2 adrenergic receptor-Gs… · the same entry in another collection · chain R against R, TM-score 1.00
- P62871 · 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
- P07550 · AlphaFold monomer V2.0 prediction for beta-2 adrenergic receptor (P07550) · a predicted model of the same protein · chain R against A, TM-score 0.92
- P63212 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain G against A, TM-score 0.63
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 P63092
- Every structure of UniProt P62871
- Every structure of UniProt P63212
- Every structure of UniProt P07550
- Elsewhere: RCSB PDB 7DHI · PDBe 7DHI · UniProt P63092 · UniProt P62871 · UniProt P63212 · UniProt P07550
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