1mqg

Crystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Iodo-Willardiine at 2.15 Angstroms Resolution

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: REASONABLE

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

glutamate receptor 2

Rattus norvegicus

UniProt P19491

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 413–527 Chain B; UniProt 413–527 Chain A; UniProt 653–796 Chain B; UniProt 653–796 Fragment:ligand binding core (S1S2J) SO4 SULFATE ION × 2 IWD 2-AMINO-3-(5-IODO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;277 K;PEG 1000, Phosphate-citrate buffer, Li sulfate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.15 Å R-free 0.233

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.

333 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–263; UniProt 653–796 Author chain B; PDBConstruct 120–263; UniProt 653–796

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 1mqg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mqg
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1mqg
Deposition date deposition_date2002-09-16
Structure title titleCrystal Structure of the GluR2 Ligand Binding Core (S1S2J) in Complex with Iodo-Willardiine at 2.15 Angstroms Resolution
Keywords keywordsionotropic glutamate receptor, GluR2, ligand binding core, S1S2, partial agonist, willardiines, iodo-willardiine, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.36
Radius of gyration Rg (electron density) rg_electron26.74
Forward intensity I(0) i054219900.00
Molecular weight molecular_weight56780.0 kDa
Excluded volume excluded_volume70706 ų
Envelope volume envelope_volume87579 ų
Hydration-shell volume shell_volume27895 ų
Envelope diameter envelope_diameter87.9
Shell Rg shell_rg33.52
Envelope Rg envelope_rg26.54
Shape Rg shape_rg26.76
Total Rg total_rg27.41
Total atoms total_atoms3968
Residues n_residues519
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 dmax85.8
Rg (real space) rg_real27.37
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real5.4220e+07
I(0) uncertainty (real space) i0_real_error7.1500e+05
Rg (reciprocal space) rg_reciprocal27.37
I(0) (reciprocal space) i0_reciprocal54220000.0000
Solution quality estimate total_estimate0.7365
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13700000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 0.267; Positv: 1.000; Valcen: 0.985; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mqga_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd1mqgb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

CATH v4.4 (4 domains)

Domain ID domain_id1mqgA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id1mqgA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id1mqgB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id1mqgB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (2)

9. Files and Curves (10)