9ijr

Cryo-EM structure of the orphan GPR52 beta-arrestin 1 complex bound to ligand c17

Method: ELECTRON MICROSCOPY Dmax: 122.7 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 EN6 N-(2-hydroxyethyl)-5-(hydroxymethyl)-3-methyl-1-[2-[[3-(trifluoromethyl)phenyl]methyl]-1-benzothiophen-7-yl]pyrazole-4-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 2–356 Not recorded G-protein coupled receptor 52 × 1 (Q9Y2T5) scFv30 antibody × 1 EN6 N-(2-hydroxyethyl)-5-(hydroxymethyl)-3-methyl-1-[2-[[3-(trifluoromethyl)phenyl]methyl]-1-benzothiophen-7-yl]pyrazole-4-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 39–393; UniProt 2–356

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 9ijr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ijr
Deposition date deposition_date2024-06-25
Structure title titleCryo-EM structure of the orphan GPR52 beta-arrestin 1 complex bound to ligand c17
Keywords keywordsComplex, membrane protein, GPCR, arrestin, beta-arrestin1, 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_guinier35.30
Radius of gyration Rg (electron density) rg_electron35.01
Forward intensity I(0) i0115393000.00
Molecular weight molecular_weight86617.0 kDa
Excluded volume excluded_volume108610 ų
Envelope volume envelope_volume149980 ų
Hydration-shell volume shell_volume38059 ų
Envelope diameter envelope_diameter128.8
Shell Rg shell_rg38.72
Envelope Rg envelope_rg34.59
Shape Rg shape_rg35.04
Total Rg total_rg35.21
Total atoms total_atoms6131
Residues n_residues866
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 dmax122.7
Rg (real space) rg_real35.45
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.1540e+08
I(0) uncertainty (real space) i0_real_error1.8610e+06
Rg (reciprocal space) rg_reciprocal35.36
I(0) (reciprocal space) i0_reciprocal115400000.0000
Solution quality estimate total_estimate0.8675
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.436
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15890000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)