8w1v

The beta2 adrenergic receptor bound to a bitopic ligand

Method: X-RAY DIFFRACTION Dmax: 114.9 Å Quality: EXCELLENT

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–161 Chain B; UniProt 2–161 Mutation:N187E,C1054T,C1097A Nanobody60 × 2 A1AE2 (2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol × 2 AV0 Lauryl Maltose Neopentyl Glycol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;100 mM Tris buffer (pH 8.0), 100 to 175 mM lithium sulfate, 38% to 42% PEG400, and 10 mM EDTA Resolution 3.00 Å R-free 0.292

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 390–549; UniProt 2–161 Author chain B; PDBConstruct 390–549; UniProt 2–161

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–365 Chain B; UniProt 1–365 Mutation:N187E,C1054T,C1097A Nanobody60 × 2 A1AE2 (2S)-1-[(3-{1-[4-(4-{(2S)-2-hydroxy-3-[(propan-2-yl)amino]propoxy}phenyl)butyl]-1H-1,2,3-triazol-4-yl}propyl)amino]-3-(2-propylphenoxy)propan-2-ol × 2 AV0 Lauryl Maltose Neopentyl Glycol × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;100 mM Tris buffer (pH 8.0), 100 to 175 mM lithium sulfate, 38% to 42% PEG400, and 10 mM EDTA Resolution 3.00 Å R-free 0.292

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 25–389; UniProt 1–365 Author chain B; PDBConstruct 25–389; UniProt 1–365

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 8w1v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w1v
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8w1v
Deposition date deposition_date2024-02-19
Structure title titleThe beta2 adrenergic receptor bound to a bitopic ligand
Keywords keywordssignal transduction, bitopic ligand, , SIGNALING PROTEIN, GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.78
Radius of gyration Rg (electron density) rg_electron35.88
Forward intensity I(0) i0221678000.00
Molecular weight molecular_weight126570.0 kDa
Excluded volume excluded_volume161080 ų
Envelope volume envelope_volume209460 ų
Hydration-shell volume shell_volume48663 ų
Envelope diameter envelope_diameter119.7
Shell Rg shell_rg42.21
Envelope Rg envelope_rg35.38
Shape Rg shape_rg35.86
Total Rg total_rg36.40
Total atoms total_atoms8913
Residues n_residues1118
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 dmax114.9
Rg (real space) rg_real36.59
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real2.2170e+08
I(0) uncertainty (real space) i0_real_error3.7030e+06
Rg (reciprocal space) rg_reciprocal36.71
I(0) (reciprocal space) i0_reciprocal221700000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.1
Skewness Skewness skewness0.080
Kurtosis Kurtosis kurtosis-0.574
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14270000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)