8wu1

Cryo-EM structure of CB1-beta-arrestin1 complex

Method: ELECTRON MICROSCOPY Dmax: 139.4 Å Quality: REASONABLE

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

Beta-arrestin-1

Bos taurus

UniProt P17870

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 C; UniProt 1–393 Mutation:R169E, I386A, V387A, F388A Fab30 heavy chain × 1 Fab30 light chain × 1 Cannabinoid receptor 1,Vasopressin V2 receptor × 1 (P21554,P30518) KCA methyl N-{1-[(4-fluorophenyl)methyl]-1H-indazole-3-carbonyl}-3-methyl-L-valinate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

23 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–393; UniProt 1–393

Cannabinoid receptor 1,Vasopressin V2 receptor

Homo sapiens

UniProt P21554

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 R; UniProt 1–413 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P17870) Fab30 heavy chain × 1 Fab30 light chain × 1 KCA methyl N-{1-[(4-fluorophenyl)methyl]-1H-indazole-3-carbonyl}-3-methyl-L-valinate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNR1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 1–413; UniProt 1–413

Cannabinoid receptor 1,Vasopressin V2 receptor

Homo sapiens

UniProt P30518

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 R; UniProt 342–371 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P17870) Fab30 heavy chain × 1 Fab30 light chain × 1 KCA methyl N-{1-[(4-fluorophenyl)methyl]-1H-indazole-3-carbonyl}-3-methyl-L-valinate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

36 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V2R_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 414–443; UniProt 342–371

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 8wu1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wu1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wu1
Deposition date deposition_date2023-10-19
Structure title titleCryo-EM structure of CB1-beta-arrestin1 complex
Keywords keywordscannabinoid receptor, arrestin, biased signal, class A GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.45
Radius of gyration Rg (electron density) rg_electron40.91
Forward intensity I(0) i0157119000.00
Molecular weight molecular_weight102810.0 kDa
Excluded volume excluded_volume129280 ų
Envelope volume envelope_volume185200 ų
Hydration-shell volume shell_volume40860 ų
Envelope diameter envelope_diameter149.4
Shell Rg shell_rg41.56
Envelope Rg envelope_rg41.35
Shape Rg shape_rg40.94
Total Rg total_rg40.87
Total atoms total_atoms7250
Residues n_residues1008
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 dmax139.4
Rg (real space) rg_real40.79
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.5710e+08
I(0) uncertainty (real space) i0_real_error3.1000e+06
Rg (reciprocal space) rg_reciprocal40.45
I(0) (reciprocal space) i0_reciprocal157100000.0000
Solution quality estimate total_estimate0.6025
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary39.3
Skewness Skewness skewness0.580
Kurtosis Kurtosis kurtosis-0.045
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11640000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 0.107; Positv: 1.000; Valcen: 0.741; Smooth: 0.369

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)