7epd

Cryo-EM structure of inactive mGlu2-7 heterodimer

Method: ELECTRON MICROSCOPY Dmax: 172.2 Å Quality: REASONABLE

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

Metabotropic glutamate receptor 2,Peptidylprolyl isomerase

Homo sapiens

UniProt Q0VDC6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 39–145 Mutation:N655Y,H815Y Isoform 3 of Metabotropic glutamate receptor 7 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q0VDC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 821–927; UniProt 39–145

Metabotropic glutamate receptor 2,Peptidylprolyl isomerase

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–825 Mutation:N655Y,H815Y Isoform 3 of Metabotropic glutamate receptor 7 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 A; PDBConstruct 11–817; UniProt 19–825

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 7epd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7epd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7epd
Deposition date deposition_date2021-04-26
Structure title titleCryo-EM structure of inactive mGlu2-7 heterodimer
Keywords keywordsCryo-EM structure, membrane protein, GPCR; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.59
Radius of gyration Rg (electron density) rg_electron55.24
Forward intensity I(0) i0372976000.00
Molecular weight molecular_weight151740.0 kDa
Excluded volume excluded_volume185910 ų
Envelope volume envelope_volume321870 ų
Hydration-shell volume shell_volume50809 ų
Envelope diameter envelope_diameter180.9
Shell Rg shell_rg54.61
Envelope Rg envelope_rg54.81
Shape Rg shape_rg55.40
Total Rg total_rg54.70
Total atoms total_atoms10710
Residues n_residues1569
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 dmax172.2
Rg (real space) rg_real56.11
Rg uncertainty (real space) rg_real_error1.82
I(0) (real space) i0_real3.7300e+08
I(0) uncertainty (real space) i0_real_error7.9910e+06
Rg (reciprocal space) rg_reciprocal55.10
I(0) (reciprocal space) i0_reciprocal372400000.0000
Solution quality estimate total_estimate0.5688
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.765
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15680000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.763; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7epdA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (1)

9. Files and Curves (10)