5cnj

mGlur2 with glutamate analog

Method: X-RAY DIFFRACTION Dmax: 96.0 Å Quality: EXCELLENT

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–493 Chain B; UniProt 2–493 Fragment:UNP residues 2-493 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 52Q (1R,2S,4R,5R,6R)-2-amino-4-(1H-1,2,4-triazol-3-ylsulfanyl)bicyclo[3.1.0]hexane-2,6-dicarboxylic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;295 K;100mM Hepes pH 7 + 20% PEG 3350 + 200mM Magnesium Chloride Resolution 2.65 Å R-free 0.241

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 4–495; UniProt 2–493 Author chain B; PDBConstruct 4–495; UniProt 2–493

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 5cnj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5cnj
Deposition date deposition_date2015-07-17
Structure title titlemGlur2 with glutamate analog
Keywords keywordsglutamate receptor analog, 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_guinier30.71
Radius of gyration Rg (electron density) rg_electron29.61
Forward intensity I(0) i0160258000.00
Molecular weight molecular_weight99647.0 kDa
Excluded volume excluded_volume124320 ų
Envelope volume envelope_volume154060 ų
Hydration-shell volume shell_volume42117 ų
Envelope diameter envelope_diameter101.5
Shell Rg shell_rg37.85
Envelope Rg envelope_rg29.75
Shape Rg shape_rg29.62
Total Rg total_rg30.30
Total atoms total_atoms7037
Residues n_residues890
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 dmax96.0
Rg (real space) rg_real30.59
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.6030e+08
I(0) uncertainty (real space) i0_real_error2.2770e+06
Rg (reciprocal space) rg_reciprocal30.64
I(0) (reciprocal space) i0_reciprocal160300000.0000
Solution quality estimate total_estimate0.9032
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45750000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5cnja_
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
Domain ID domain_idd5cnjb_
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 (4 domains)

Domain ID domain_id5cnjA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id5cnjA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id5cnjB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id5cnjB02
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)