8vj9

CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted

Method: ELECTRON MICROSCOPY Dmax: 113.0 Å Quality: GOOD

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

Atypical chemokine receptor 3

Homo sapiens

UniProt P25106

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 2–362 Non-standard monomer:Yes (specific site not provided by mmCIF) Fab7 heavy chain × 1 Fab7 light chain × 1 Beta-arrestin-2 × 1 (P32120) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACKR3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 4–364; UniProt 2–362

Beta-arrestin-2

Bos taurus

UniProt P32120

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–392 Fragment:Arrestin3 variant with the C edge loop from Arrestin2 inserted Fab7 heavy chain × 1 Fab7 light chain × 1 Atypical chemokine receptor 3 × 1 (P25106) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB2_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–389; UniProt 1–392

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 8vj9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vj9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8vj9
Deposition date deposition_date2024-01-06
Structure title titleCryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted
Keywords keywordsGPCR, arrestin, signaling, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.02
Radius of gyration Rg (electron density) rg_electron34.06
Forward intensity I(0) i093523800.00
Molecular weight molecular_weight78236.0 kDa
Excluded volume excluded_volume98495 ų
Envelope volume envelope_volume131300 ų
Hydration-shell volume shell_volume34572 ų
Envelope diameter envelope_diameter115.0
Shell Rg shell_rg37.95
Envelope Rg envelope_rg33.91
Shape Rg shape_rg34.02
Total Rg total_rg34.50
Total atoms total_atoms10983
Residues n_residues703
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 dmax113.0
Rg (real space) rg_real34.17
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real9.3520e+07
I(0) uncertainty (real space) i0_real_error1.7460e+06
Rg (reciprocal space) rg_reciprocal34.08
I(0) (reciprocal space) i0_reciprocal93520000.0000
Solution quality estimate total_estimate0.8686
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.1
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10990000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)