8t6j

CDPPB-bound inactive mGlu5

Method: ELECTRON MICROSCOPY Dmax: 179.7 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 20–876 Chain B; UniProt 20–876 Not recorded YKU 3-cyano-N-(1,3-diphenyl-1H-pyrazol-5-yl)benzamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 8t6j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t6j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t6j
Deposition date deposition_date2023-06-16
Structure title titleCDPPB-bound inactive 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_guinier59.30
Radius of gyration Rg (electron density) rg_electron60.74
Forward intensity I(0) i0384942000.00
Molecular weight molecular_weight166330.0 kDa
Excluded volume excluded_volume208830 ų
Envelope volume envelope_volume362030 ų
Hydration-shell volume shell_volume52333 ų
Envelope diameter envelope_diameter189.5
Shell Rg shell_rg59.68
Envelope Rg envelope_rg57.77
Shape Rg shape_rg60.78
Total Rg total_rg60.58
Total atoms total_atoms11670
Residues n_residues1534
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 dmax179.7
Rg (real space) rg_real59.85
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real3.8490e+08
I(0) uncertainty (real space) i0_real_error8.3020e+06
Rg (reciprocal space) rg_reciprocal58.77
I(0) (reciprocal space) i0_reciprocal384300000.0000
Solution quality estimate total_estimate0.7961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.3
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.870
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12030000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.733; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (2)

9. Files and Curves (10)