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Cryo-EM structure of the full agonist isoprenaline-bound BETA2 adrenergic receptor-gs protein complex.

Analyse Cryo-EM structure of the full agonist isoprenaline-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: 7DHR
Type: protein
Length: 977 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: 5FW
Pockets: 15 · best druggability 0.78

Structure

electron microscopy · 5 distinct chains · 23% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanine nucleotide-binding protein G(S) subunit alpha isoforms short	protein	194	35% helix, 15% strand	P63092
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	327	3% helix, 32% strand	P62871
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	49	43% helix, 0% strand	P63212
N	NB35 nanobody	protein	123	0% helix, 26% strand	—
R	Beta-2 adrenergic receptor	protein	284	44% helix, 0% strand	P07550

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

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	586	0.78	0.84	54	empty
2	338	0.77	0.87	36	5FW
3	223	0.74	0.89	27	empty
4	1183	0.73	0.76	85	empty
5	275	0.68	0.84	40	empty

Interfaces

7 interfaces between chains.

B–G · 1605 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 1465 Å² buried · 4 hydrogen bonds · protein-protein
A–R · 1271 Å² buried · 5 hydrogen bonds · protein-protein
A–N · 676 Å² buried · 2 hydrogen bonds · protein-protein
B–N · 489 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7DHR · Cryo-EM structure of the full agonist isoprenaline-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 0.60

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 7DHR · PDBe 7DHR · UniProt P63092 · UniProt P62871 · UniProt P63212 · UniProt P07550

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