8t7h

Quis-bound intermediate mGlu5

Method: ELECTRON MICROSCOPY Dmax: 196.9 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 20–876 Chain B; UniProt 20–876 Not recorded Nanobody 43 × 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 3.30 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 25–881; UniProt 20–876 Author chain B; PDBConstruct 25–881; UniProt 20–876

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 8t7h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t7h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t7h
Deposition date deposition_date2023-06-20
Structure title titleQuis-bound intermediate mGlu5
Keywords keywordsGPCR, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.60
Radius of gyration Rg (electron density) rg_electron60.89
Forward intensity I(0) i0523435000.00
Molecular weight molecular_weight186350.0 kDa
Excluded volume excluded_volume231050 ų
Envelope volume envelope_volume376280 ų
Hydration-shell volume shell_volume56329 ų
Envelope diameter envelope_diameter208.3
Shell Rg shell_rg54.93
Envelope Rg envelope_rg60.76
Shape Rg shape_rg61.02
Total Rg total_rg60.28
Total atoms total_atoms13100
Residues n_residues1794
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 dmax196.9
Rg (real space) rg_real60.58
Rg uncertainty (real space) rg_real_error2.01
I(0) (real space) i0_real5.2340e+08
I(0) uncertainty (real space) i0_real_error1.0970e+07
Rg (reciprocal space) rg_reciprocal58.73
I(0) (reciprocal space) i0_reciprocal521900000.0000
Solution quality estimate total_estimate0.7532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.564
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha17250000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.645; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.821; Smooth: 0.032

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)