8x0h

Human FL Metabotropic glutamate receptor 5, mGlu5-5M with quisqualate, Rcc conformation

Method: ELECTRON MICROSCOPY Dmax: 169.5 Å Quality: GOOD

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

Metabotropic glutamate receptor 5

Homo sapiens

UniProt P41594

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–856 Chain B; UniProt 21–856 Mutation:T742A, S753A, T777A, I799A, A813L,N445A,H350L NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–836; UniProt 21–856 Author chain B; PDBConstruct 1–836; UniProt 21–856

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 8x0h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x0h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x0h
Deposition date deposition_date2023-11-04
Structure title titleHuman FL Metabotropic glutamate receptor 5, mGlu5-5M with quisqualate, Rcc conformation
Keywords keywordsG-PROTEIN COUPLED RECEPTORS, SIGNAL TRANSDUCTION, METABOTROPIC GLUTAMATE RECEPTOR, Agonist, active state, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.06
Radius of gyration Rg (electron density) rg_electron58.71
Forward intensity I(0) i0418656000.00
Molecular weight molecular_weight175780.0 kDa
Excluded volume excluded_volume221830 ų
Envelope volume envelope_volume355790 ų
Hydration-shell volume shell_volume52193 ų
Envelope diameter envelope_diameter181.2
Shell Rg shell_rg58.52
Envelope Rg envelope_rg56.81
Shape Rg shape_rg58.68
Total Rg total_rg58.78
Total atoms total_atoms12317
Residues n_residues1558
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 dmax169.5
Rg (real space) rg_real57.61
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.1870e+08
I(0) uncertainty (real space) i0_real_error7.9790e+06
Rg (reciprocal space) rg_reciprocal56.54
I(0) (reciprocal space) i0_reciprocal418000000.0000
Solution quality estimate total_estimate0.7825
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.4
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.891
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12260000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.663; 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)