9uyh

Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 1)

Method: ELECTRON MICROSCOPY Dmax: 122.8 Å Quality: GOOD

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

Retinoic acid receptor responder protein 2

Homo sapiens

UniProt Q99969

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 L; UniProt 20–157 Not recorded Beta-arrestin-1 × 1 (P49407) Nanobody 32 × 1 Chemerin-like receptor 2,Vasopressin V2 receptor × 1 (P46091,P30518) Single-chain fragment variable 30 (scFv30) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RARR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 16–153; UniProt 20–157

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 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–376 Mutation:C59A, C125S, C140I, C150V, R169E, C242V, C251V and C269S Retinoic acid receptor responder protein 2 × 1 (Q99969) Nanobody 32 × 1 Chemerin-like receptor 2,Vasopressin V2 receptor × 1 (P46091,P30518) Single-chain fragment variable 30 (scFv30) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 A; PDBConstruct 1–376; UniProt 1–376

Chemerin-like receptor 2,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 343–371 Non-standard monomer:Yes (specific site not provided by mmCIF) Retinoic acid receptor responder protein 2 × 1 (Q99969) Beta-arrestin-1 × 1 (P49407) Nanobody 32 × 1 Single-chain fragment variable 30 (scFv30) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 368–396; UniProt 343–371

Chemerin-like receptor 2,Vasopressin V2 receptor

Homo sapiens

UniProt P46091

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 2–322 Non-standard monomer:Yes (specific site not provided by mmCIF) Retinoic acid receptor responder protein 2 × 1 (Q99969) Beta-arrestin-1 × 1 (P49407) Nanobody 32 × 1 Single-chain fragment variable 30 (scFv30) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CML2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 47–367; UniProt 2–322

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 9uyh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uyh
Deposition date deposition_date2025-05-15
Structure title titleCryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 1)
Keywords keywords;G protein-coupled receptor 1, chemerin, beta-arrestin1, signaling protein, 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_guinier36.66
Radius of gyration Rg (electron density) rg_electron36.46
Forward intensity I(0) i0152194000.00
Molecular weight molecular_weight101530.0 kDa
Excluded volume excluded_volume127940 ų
Envelope volume envelope_volume171630 ų
Hydration-shell volume shell_volume40970 ų
Envelope diameter envelope_diameter131.2
Shell Rg shell_rg40.65
Envelope Rg envelope_rg36.40
Shape Rg shape_rg36.49
Total Rg total_rg36.67
Total atoms total_atoms7176
Residues n_residues960
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 dmax122.8
Rg (real space) rg_real36.79
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real1.5220e+08
I(0) uncertainty (real space) i0_real_error2.5340e+06
Rg (reciprocal space) rg_reciprocal36.71
I(0) (reciprocal space) i0_reciprocal152200000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.391
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25820000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.887; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)