Research workbench
Isoproterenol bound BETA1 adrenergic receptor in complex with heterotrimeric gi protein
Analyse Isoproterenol bound BETA1 adrenergic receptor in complex with heterotrimeric gi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S0F
- Type
- protein
- Length
- 892 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BETA1-adrenergic receptor; Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit…
- UniProt
- P62871, P10824, P63212
- Ligands
- 5FW
- Pockets
- 7 · best druggability 0.82
Structure
electron microscopy · 4 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | BETA1-adrenergic receptor | protein | 272 | 80% helix, 0% strand | — |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 338 | 7% helix, 47% strand | P62871 |
| A | Guanine nucleotide-binding protein G(I) subunit alpha-1, | protein | 222 | 44% helix, 18% strand | P10824 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 60 | 58% helix, 3% strand | P63212 |
Ligands and binding sites
- 5FW · Isoprenaline · ligand · chains R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 843 | 0.82 | 0.85 | 63 | empty |
| 2 | 919 | 0.76 | 0.79 | 85 | empty |
| 3 | 246 | 0.75 | 0.89 | 34 | 5FW |
| 4 | 198 | 0.48 | 0.75 | 25 | empty |
| 5 | 118 | 0.44 | 0.77 | 19 | empty |
Interfaces
5 interfaces between chains.
- B–G · 2305 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 1152 Ų buried · 10 hydrogen bonds · protein-protein
- R–A · 1014 Ų buried · 7 hydrogen bonds · protein-protein
- R–B · 43 Ų buried · 0 hydrogen bonds · protein-protein
- A–G · 14 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7S0F · Isoproterenol bound beta1 adrenergic receptor in complex with heterotrimeric Gi protein · 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
- P10824 · 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 0.83
- 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 P62871
- Every structure of UniProt P10824
- Every structure of UniProt P63212
- Elsewhere: RCSB PDB 7S0F · PDBe 7S0F · UniProt P62871 · UniProt P10824 · UniProt P63212
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