9ijs

Cryo-EM structure of the orphan GPR52 bound to beta-arrestin 1 in ligand-free state

Method: ELECTRON MICROSCOPY Dmax: 118.3 Å Quality: GOOD

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

G-protein coupled receptor 52

Homo sapiens

UniProt Q9Y2T5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: tetrameric(4) Count mismatch; review required Chain A; UniProt 1–340 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P49407) scFv30 antibody × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GPR52_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 1–340

Beta-arrestin-1

Homo sapiens

UniProt P49407

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 3 PDB declaration: tetrameric(4) Count mismatch; review required Chain C; UniProt 2–393 Not recorded G-protein coupled receptor 52 × 1 (Q9Y2T5) scFv30 antibody × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 11–402; UniProt 2–393

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 9ijs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ijs
Deposition date deposition_date2024-06-25
Structure title titleCryo-EM structure of the orphan GPR52 bound to beta-arrestin 1 in ligand-free state
Keywords keywordsComplex, membrane protein, GPCR, arrestin, MEMBRANE PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM complex; MEMBRANE PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.81
Radius of gyration Rg (electron density) rg_electron34.48
Forward intensity I(0) i0111602000.00
Molecular weight molecular_weight85838.0 kDa
Excluded volume excluded_volume107970 ų
Envelope volume envelope_volume147800 ų
Hydration-shell volume shell_volume37829 ų
Envelope diameter envelope_diameter125.2
Shell Rg shell_rg38.60
Envelope Rg envelope_rg34.13
Shape Rg shape_rg34.50
Total Rg total_rg34.73
Total atoms total_atoms6074
Residues n_residues850
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 dmax118.3
Rg (real space) rg_real34.95
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real1.1160e+08
I(0) uncertainty (real space) i0_real_error2.0160e+06
Rg (reciprocal space) rg_reciprocal34.87
I(0) (reciprocal space) i0_reciprocal111600000.0000
Solution quality estimate total_estimate0.8741
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14560000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)