Structure of beta2 adrenergic receptor fused to a Gs peptide

Experimental Data Snapshot

  • Resolution: 3.70 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.279 

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Structural Insights into the Process of GPCR-G Protein Complex Formation.

Liu, X.Xu, X.Hilger, D.Aschauer, P.Tiemann, J.K.S.Du, Y.Liu, H.Hirata, K.Sun, X.Guixa-Gonzalez, R.Mathiesen, J.M.Hildebrand, P.W.Kobilka, B.K.

(2019) Cell 177: 1243-1251.e12

  • DOI: https://doi.org/10.1016/j.cell.2019.04.021
  • Primary Citation of Related Structures:  
    6E67, 6EG8

  • PubMed Abstract: 

    The crystal structure of the β2-adrenergic receptor (β2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (β2AR-Gs empty ). Unfortunately, the β2AR-Gs empty complex does not provide a clear explanation for G protein coupling specificity. Evidence from several sources suggests the existence of a transient complex between the β2AR and GDP-bound Gs protein (β2AR-Gs GDP ) that may represent an intermediate on the way to the formation of β2AR-Gs empty and may contribute to coupling specificity. Here we present a structure of the β2AR in complex with the carboxyl terminal 14 amino acids from Gαs along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the β2AR and Gs that may represent an intermediate that contributes to Gs coupling specificity.

  • Organizational Affiliation

    Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Medicine, Tsinghua University, Beijing 100084, China. Electronic address: liu_xy@mail.tsinghua.edu.cn.

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Beta-2 adrenergic receptor chimera
A, B
531Homo sapiensEnterobacteria phage RB59Mutation(s): 8 
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for P07550 (Homo sapiens)
Explore P07550 
Go to UniProtKB:  P07550
PHAROS:  P07550
GTEx:  ENSG00000169252 
Find proteins for P63092 (Homo sapiens)
Explore P63092 
Go to UniProtKB:  P63092
PHAROS:  P63092
GTEx:  ENSG00000087460 
Find proteins for A0A097J809 (Enterobacteria phage RB59)
Explore A0A097J809 
Go to UniProtKB:  A0A097J809
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsA0A097J809P63092P07550
Sequence Annotations
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
Query on P0G

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
C21 H26 N2 O4
Binding Affinity Annotations 
IDSourceBinding Affinity
P0G BindingDB:  6E67 EC50: 0.1 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Resolution: 3.70 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.279 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.01α = 90
b = 377.44β = 90
c = 45.59γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling

Structure Validation

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Ligand Structure Quality Assessment 

Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-06-05
    Type: Initial release
  • Version 1.1: 2023-10-11
    Changes: Data collection, Database references, Refinement description