8wgc

heterodimer of mGlu2 and mGlu4 bound with mGlu2 agonist LY379268

Method: ELECTRON MICROSCOPY Dmax: 171.3 Å Quality: REASONABLE

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

Metabotropic glutamate receptor 2

Homo sapiens

UniProt Q14416

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 19–872 Not recorded Metabotropic glutamate receptor 4 × 1 (Q14833) W92 (1R,4R,5S,6R)-4-azanyl-2-oxabicyclo[3.1.0]hexane-4,6-dicarboxylic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.95 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 1–854; UniProt 19–872

Metabotropic glutamate receptor 4

Homo sapiens

UniProt Q14833

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 33–912 Not recorded Metabotropic glutamate receptor 2 × 1 (Q14416) W92 (1R,4R,5S,6R)-4-azanyl-2-oxabicyclo[3.1.0]hexane-4,6-dicarboxylic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.95 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–880; UniProt 33–912

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 8wgc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wgc
Deposition date deposition_date2023-09-20
Structure title titleheterodimer of mGlu2 and mGlu4 bound with mGlu2 agonist LY379268
Keywords keywordsGPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.79
Radius of gyration Rg (electron density) rg_electron58.26
Forward intensity I(0) i0285659000.00
Molecular weight molecular_weight86804.0 kDa
Excluded volume excluded_volume85333 ų
Envelope volume envelope_volume266350 ų
Hydration-shell volume shell_volume40709 ų
Envelope diameter envelope_diameter183.9
Shell Rg shell_rg57.48
Envelope Rg envelope_rg54.19
Shape Rg shape_rg58.27
Total Rg total_rg58.23
Total atoms total_atoms6193
Residues n_residues1545
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 dmax171.3
Rg (real space) rg_real58.23
Rg uncertainty (real space) rg_real_error1.94
I(0) (real space) i0_real2.8570e+08
I(0) uncertainty (real space) i0_real_error5.8690e+06
Rg (reciprocal space) rg_reciprocal57.35
I(0) (reciprocal space) i0_reciprocal285300000.0000
Solution quality estimate total_estimate0.5563
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary44.4
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.985
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8788000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 0.009; Positv: 1.000; Valcen: 0.705; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)