5kzn

Metabotropic Glutamate Receptor

Method: X-RAY DIFFRACTION Dmax: 108.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–564 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;100mM Tris HCl pH 8.5,.5% PEG MME 5K, 800mM Potassium Sodium Tartrate Resolution 2.80 Å R-free 0.249

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 1–564; UniProt 1–564

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 5kzn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5kzn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5kzn
Deposition date deposition_date2016-07-25
Structure title titleMetabotropic Glutamate Receptor
Keywords keywordsmGluR2, antagonist, antidepressent, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.14
Radius of gyration Rg (electron density) rg_electron27.35
Forward intensity I(0) i050769400.00
Molecular weight molecular_weight54909.0 kDa
Excluded volume excluded_volume68385 ų
Envelope volume envelope_volume86866 ų
Hydration-shell volume shell_volume27598 ų
Envelope diameter envelope_diameter115.5
Shell Rg shell_rg32.79
Envelope Rg envelope_rg28.22
Shape Rg shape_rg27.32
Total Rg total_rg28.03
Total atoms total_atoms3872
Residues n_residues503
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 dmax108.4
Rg (real space) rg_real28.37
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real5.0770e+07
I(0) uncertainty (real space) i0_real_error9.6030e+05
Rg (reciprocal space) rg_reciprocal28.29
I(0) (reciprocal space) i0_reciprocal50770000.0000
Solution quality estimate total_estimate0.7930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.572
Kurtosis Kurtosis kurtosis0.084
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9157000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.577; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.619; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)