Research workbench
Structural basis of the activation of heterotrimeric gs-protein by isoproterenol-bound BETA1-adrenergic receptor
Analyse Structural basis of the activation of heterotrimeric gs-protein by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JJO
- Type
- protein
- Length
- 1,002 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1; Nanobody 35; Guanine…
- UniProt
- P62871, P04896, P63212
- Ligands
- 5FW
- Pockets
- 16 · best druggability 0.81
Structure
electron microscopy · 5 distinct chains · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 338 | 7% helix, 48% strand | P62871 |
| N | Nanobody 35 | protein | 128 | 7% helix, 45% strand | — |
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 200 | 47% helix, 20% strand | P04896 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 57 | 53% helix, 0% strand | P63212 |
| R | BETA1-adrenergic receptor | protein | 279 | 83% helix, 0% strand | — |
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
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 740 | 0.81 | 0.85 | 57 | empty |
| 2 | 1006 | 0.77 | 0.79 | 76 | empty |
| 3 | 264 | 0.71 | 0.86 | 37 | 5FW |
| 4 | 185 | 0.69 | 0.87 | 29 | empty |
| 5 | 169 | 0.67 | 0.86 | 28 | empty |
Interfaces
6 interfaces between chains.
- B–G · 2218 Ų buried · 16 hydrogen bonds · protein-protein
- B–A · 1445 Ų buried · 17 hydrogen bonds · protein-protein
- A–R · 1154 Ų buried · 8 hydrogen bonds · protein-protein
- N–A · 960 Ų buried · 13 hydrogen bonds · protein-protein
- B–N · 449 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7JJO · Structural Basis of the Activation of Heterotrimeric Gs-protein by Isoproterenol-bound… · 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
- P04896 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(S) 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 0.62
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 P04896
- Every structure of UniProt P63212
- Elsewhere: RCSB PDB 7JJO · PDBe 7JJO · UniProt P62871 · UniProt P04896 · UniProt P63212
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