8wgd

mGlu2-4 inactive heterodimer

Method: ELECTRON MICROSCOPY Dmax: 178.5 Å Quality: GOOD

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 C; UniProt 19–872 Not recorded Metabotropic glutamate receptor 4 × 1 (Q14833) WAG (1S,2R)-2-[(2S)-2-azanyl-1-oxidanyl-1-oxidanylidene-3-(9H-xanthen-9-yl)propan-2-yl]cyclopropane-1-carboxylic acid × 1 WA6 (2S)-2-azanyl-2-cyclopropyl-2-(4-phosphonophenyl)ethanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.45 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 C; 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 B; UniProt 33–912 Not recorded Metabotropic glutamate receptor 2 × 1 (Q14416) WAG (1S,2R)-2-[(2S)-2-azanyl-1-oxidanyl-1-oxidanylidene-3-(9H-xanthen-9-yl)propan-2-yl]cyclopropane-1-carboxylic acid × 1 WA6 (2S)-2-azanyl-2-cyclopropyl-2-(4-phosphonophenyl)ethanoic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.45 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 B; 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 8wgd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wgd
Deposition date deposition_date2023-09-20
Structure title titlemGlu2-4 inactive heterodimer
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_guinier57.45
Radius of gyration Rg (electron density) rg_electron57.93
Forward intensity I(0) i0351244000.00
Molecular weight molecular_weight82066.0 kDa
Excluded volume excluded_volume68067 ų
Envelope volume envelope_volume250790 ų
Hydration-shell volume shell_volume38864 ų
Envelope diameter envelope_diameter179.8
Shell Rg shell_rg56.48
Envelope Rg envelope_rg53.58
Shape Rg shape_rg57.93
Total Rg total_rg57.90
Total atoms total_atoms6076
Residues n_residues1508
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 dmax178.5
Rg (real space) rg_real57.90
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real3.5120e+08
I(0) uncertainty (real space) i0_real_error7.4750e+06
Rg (reciprocal space) rg_reciprocal57.01
I(0) (reciprocal space) i0_reciprocal350700000.0000
Solution quality estimate total_estimate0.7726
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.3
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.976
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8754000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.703; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)