8j8v

Structure of beta-arrestin2 in complex with D6Rpp (Local Refine)

Method: ELECTRON MICROSCOPY Dmax: 134.1 Å Quality: GOOD

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

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–420 Chain F; UniProt 1–420 Mutation:C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Fab30 Heavy Chain × 2 Fab30 Light Chain × 2 Atypical chemokine receptor 2 × 2 (O00590) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 3 seconds before plunging. Resolution 3.22 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–420; UniProt 1–420 Author chain F; PDBConstruct 1–420; UniProt 1–420

Atypical chemokine receptor 2

OrganismNot specified

UniProt O00590

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 338–355 Chain H; UniProt 338–355 Fragment:C-terminal tail Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-2 × 2 (P32120) Fab30 Heavy Chain × 2 Fab30 Light Chain × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 3 seconds before plunging. Resolution 3.22 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACKR2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–18; UniProt 338–355 Author chain H; PDBConstruct 1–18; UniProt 338–355

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 8j8v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8j8v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8j8v
Deposition date deposition_date2023-05-02
Structure title titleStructure of beta-arrestin2 in complex with D6Rpp (Local Refine)
Keywords keywordsGPCR, Arrestin, SIGNALING PROTEIN, 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_guinier40.25
Radius of gyration Rg (electron density) rg_electron40.19
Forward intensity I(0) i0274633000.00
Molecular weight molecular_weight133950.0 kDa
Excluded volume excluded_volume167490 ų
Envelope volume envelope_volume235630 ų
Hydration-shell volume shell_volume51536 ų
Envelope diameter envelope_diameter140.0
Shell Rg shell_rg43.16
Envelope Rg envelope_rg39.56
Shape Rg shape_rg40.18
Total Rg total_rg40.39
Total atoms total_atoms9437
Residues n_residues1191
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 dmax134.1
Rg (real space) rg_real40.35
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real2.7460e+08
I(0) uncertainty (real space) i0_real_error4.9870e+06
Rg (reciprocal space) rg_reciprocal40.25
I(0) (reciprocal space) i0_reciprocal274600000.0000
Solution quality estimate total_estimate0.8750
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21920000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)