4xar

mGluR2 ECD and mGluR3 ECD complex with ligands

Method: X-RAY DIFFRACTION Dmax: 88.4 Å Quality: GOOD

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

Metabotropic glutamate receptor 3

Homo sapiens

UniProt Q14832

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 2–508 Fragment:UNP RESIDUES 2-508 40F (1S,2S,5R,6S)-2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 2 IOD IODIDE ION × 16 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;295 K;20% PEG 3350, 200mM Ammonium Iodide Resolution 2.26 Å R-free 0.224

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.

19 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRM3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–510; UniProt 2–508

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 4xar

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xar
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xar
Deposition date deposition_date2014-12-15
Structure title titlemGluR2 ECD and mGluR3 ECD complex with ligands
Keywords keywordsmGluR2 mGluR3 ECD, 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_guinier23.48
Radius of gyration Rg (electron density) rg_electron22.41
Forward intensity I(0) i046974200.00
Molecular weight molecular_weight51195.0 kDa
Excluded volume excluded_volume62981 ų
Envelope volume envelope_volume74907 ų
Hydration-shell volume shell_volume27344 ų
Envelope diameter envelope_diameter91.3
Shell Rg shell_rg29.93
Envelope Rg envelope_rg22.97
Shape Rg shape_rg22.34
Total Rg total_rg23.46
Total atoms total_atoms3547
Residues n_residues445
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 dmax88.4
Rg (real space) rg_real23.43
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real4.6970e+07
I(0) uncertainty (real space) i0_real_error7.7260e+05
Rg (reciprocal space) rg_reciprocal23.44
I(0) (reciprocal space) i0_reciprocal46970000.0000
Solution quality estimate total_estimate0.8165
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.072
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11710000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.558; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4xara_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamilyc.93.1 — Periplasmic binding protein-like I
Family Family familyc.93.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id4xarA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id4xarA02
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)