9w3f

Cryo-EM structure of the human beta2-adrenergic receptor in complex with a novel antagonist

Method: ELECTRON MICROSCOPY Dmax: 96.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Beta-2 adrenergic receptor,Endolysin

Homo sapiens

UniProt P00720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–162 Not recorded Beta2 adrenogic receptor inactive-state stabling nanobody Nb60 × 1 BERBERINE × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.04 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 255–415; UniProt 2–162

Beta-2 adrenergic receptor,Endolysin

Homo sapiens

UniProt P07550

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–230 Chain A; UniProt 264–365 Not recorded Beta2 adrenogic receptor inactive-state stabling nanobody Nb60 × 1 BERBERINE × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.04 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

143 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADRB2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–254; UniProt 1–230 Author chain A; PDBConstruct 416–517; UniProt 264–365

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9w3f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w3f
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9w3f
Deposition date deposition_date2025-07-29
Structure title titleCryo-EM structure of the human beta2-adrenergic receptor in complex with a novel antagonist
Keywords keywordsAntagonist, membrane protein, GPCR; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.90
Radius of gyration Rg (electron density) rg_electron26.26
Forward intensity I(0) i026489500.00
Molecular weight molecular_weight42431.0 kDa
Excluded volume excluded_volume54265 ų
Envelope volume envelope_volume64816 ų
Hydration-shell volume shell_volume22599 ų
Envelope diameter envelope_diameter98.6
Shell Rg shell_rg30.87
Envelope Rg envelope_rg26.74
Shape Rg shape_rg26.27
Total Rg total_rg26.80
Total atoms total_atoms2992
Residues n_residues393
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax96.1
Rg (real space) rg_real27.27
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real2.6490e+07
I(0) uncertainty (real space) i0_real_error4.4800e+05
Rg (reciprocal space) rg_reciprocal27.16
I(0) (reciprocal space) i0_reciprocal26490000.0000
Solution quality estimate total_estimate0.7830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.618
Kurtosis Kurtosis kurtosis-0.212
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6171000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.616; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.394; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)