9wsv

Cryo-EM structure of DAMGO-muOR-arrestin-1-Fab30 complex

Method: ELECTRON MICROSCOPY Dmax: 138.6 Å Quality: GOOD

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

Mu-type opioid receptor,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 × 5 PDB declaration: pentameric(5) 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 DAMGO × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1
Chains and sequence ranges Author chain R; PDBConstruct 351–380; UniProt 342–371

Mu-type opioid receptor,Vasopressin V2 receptor

Homo sapiens

UniProt P42866

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 6–352 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P17870) Fab30 heavy chain × 1 Fab30 light chain × 1 DAMGO × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

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

View Construct and Data Evidence
UniProt name OPRM_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 4–350; UniProt 6–352

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–393 Not recorded Mu-type opioid receptor,Vasopressin V2 receptor × 1 (P42866,P30518) Fab30 heavy chain × 1 Fab30 light chain × 1 DAMGO × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–393; UniProt 1–393

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 9wsv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wsv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9wsv
Deposition date deposition_date2025-09-15
Structure title titleCryo-EM structure of DAMGO-muOR-arrestin-1-Fab30 complex
Keywords keywordsG-protein-coupled receptors, mu-opioid receptor, single particle, Cryo-EM, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.78
Radius of gyration Rg (electron density) rg_electron41.25
Forward intensity I(0) i0174359000.00
Molecular weight molecular_weight108610.0 kDa
Excluded volume excluded_volume136620 ų
Envelope volume envelope_volume194420 ų
Hydration-shell volume shell_volume41782 ų
Envelope diameter envelope_diameter148.5
Shell Rg shell_rg42.68
Envelope Rg envelope_rg41.60
Shape Rg shape_rg41.27
Total Rg total_rg41.30
Total atoms total_atoms7635
Residues n_residues1017
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 dmax138.6
Rg (real space) rg_real41.04
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.7440e+08
I(0) uncertainty (real space) i0_real_error3.2370e+06
Rg (reciprocal space) rg_reciprocal40.78
I(0) (reciprocal space) i0_reciprocal174300000.0000
Solution quality estimate total_estimate0.8268
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis-0.200
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11850000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.798; Smooth: 0.379

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)