9ii3

Cryo-EM Structure of the 2:1 Complex of mGlu3 and beta-arrestin1

Method: ELECTRON MICROSCOPY Dmax: 212.3 Å Quality: REASONABLE

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

Metabotropic glutamate receptor 3

Homo sapiens

UniProt Q14832

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–879 Chain R; UniProt 1–879 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P49407) scFv30 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

19 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–879; UniProt 1–879 Author chain R; PDBConstruct 1–879; UniProt 1–879

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 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–418 Not recorded Metabotropic glutamate receptor 3 × 2 (Q14832) scFv30 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GLU GLUTAMIC ACID × 2 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–418; UniProt 1–418

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 9ii3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ii3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ii3
Deposition date deposition_date2024-06-19
Structure title titleCryo-EM Structure of the 2:1 Complex of mGlu3 and beta-arrestin1
Keywords keywordscomplex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier72.50
Radius of gyration Rg (electron density) rg_electron72.86
Forward intensity I(0) i0731697000.00
Molecular weight molecular_weight234080.0 kDa
Excluded volume excluded_volume295160 ų
Envelope volume envelope_volume495320 ų
Hydration-shell volume shell_volume61053 ų
Envelope diameter envelope_diameter242.9
Shell Rg shell_rg62.03
Envelope Rg envelope_rg69.84
Shape Rg shape_rg72.96
Total Rg total_rg72.27
Total atoms total_atoms16488
Residues n_residues2150
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 dmax212.3
Rg (real space) rg_real73.03
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real7.3110e+08
I(0) uncertainty (real space) i0_real_error1.6100e+07
Rg (reciprocal space) rg_reciprocal69.76
I(0) (reciprocal space) i0_reciprocal726700000.0000
Solution quality estimate total_estimate0.7319
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.973
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0023
Highest regularization parameter α highest_alpha21840000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.662; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.526; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)