Research workbench
Isoproterenol-activated dog BETA3 adrenergic receptor
Analyse Isoproterenol-activated dog BETA3 adrenergic receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7XJH
- Type
- protein
- Length
- 1,027 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, P54311, P63212, O02662
- Ligands
- 5FW
- Pockets
- 12 · best druggability 0.85
Structure
electron microscopy · 5 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 231 | 46% helix, 17% strand | P63092 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 340 | 9% helix, 45% strand | P54311 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 52 | 58% helix, 0% strand | P63212 |
| N | Nanobody-35 | protein | 128 | 5% helix, 41% strand | — |
| R | Beta-3 adrenergic receptor | protein | 276 | 80% helix, 0% strand | O02662 |
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
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 969 | 0.85 | 0.86 | 84 | empty |
| 2 | 1021 | 0.77 | 0.79 | 82 | empty |
| 3 | 211 | 0.72 | 0.88 | 40 | 5FW |
| 4 | 576 | 0.72 | 0.80 | 79 | empty |
| 5 | 648 | 0.66 | 0.75 | 59 | empty |
Interfaces
6 interfaces between chains.
- B–G · 2029 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1492 Ų buried · 18 hydrogen bonds · protein-protein
- A–R · 1345 Ų buried · 10 hydrogen bonds · protein-protein
- A–N · 756 Ų buried · 5 hydrogen bonds · protein-protein
- B–N · 426 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7XJH · Isoproterenol-activated dog beta3 adrenergic receptor · the same entry in another collection · chain R against R, TM-score 1.00
- P54311 · 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
- O02662 · AlphaFold monomer V2.0 prediction for beta-3 adrenergic receptor (O02662) · 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 0.65
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 P54311
- Every structure of UniProt P63212
- Every structure of UniProt O02662
- Elsewhere: RCSB PDB 7XJH · PDBe 7XJH · UniProt P63092 · UniProt P54311 · UniProt P63212 · UniProt O02662
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