3ijo

Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, althiazide

Method: X-RAY DIFFRACTION Dmax: 102.5 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 B; UniProt 414–527 Chain B; UniProt 653–794 Chain E; UniProt 414–527 Chain E; UniProt 653–794 Not recorded GLU GLUTAMIC ACID × 2 B4D (3S)-6-chloro-3-[(prop-2-en-1-ylsulfanyl)methyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K Resolution 2.00 Å R-free 0.234
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 414–527 Chain H; UniProt 653–794 Not recorded GLU GLUTAMIC ACID × 2 B4D (3S)-6-chloro-3-[(prop-2-en-1-ylsulfanyl)methyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;16-18 PEG8K, 0.1 M Na Cacodylate, 0.1-0.15 zinc acetate, pH 6.5, vapor diffusion, hanging drop, temperature 277K Resolution 2.00 Å R-free 0.234

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 481 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 B; PDBConstruct 1–114; UniProt 414–527 Author chain B; PDBConstruct 117–258; UniProt 653–794 Author chain E; PDBConstruct 1–114; UniProt 414–527 Author chain E; PDBConstruct 117–258; UniProt 653–794 Author chain H; PDBConstruct 1–114; UniProt 414–527 Author chain H; PDBConstruct 117–258; UniProt 653–794

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 3ijo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ijo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ijo
Deposition date deposition_date2009-08-04
Structure title titleCrystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, althiazide
Keywords keywords;glutamate receptor, glur2, AMPA receptor, neurotransmitter receptor, S1S2, allosteric modulator, Alternative splicing, Cell junction, Cell membrane, Endoplasmic reticulum, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, Membrane, Palmitate, Phosphoprotein, Postsynaptic cell membrane, Receptor, RNA editing, Synapse, Transmembrane, Transport, 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_guinier31.26
Radius of gyration Rg (electron density) rg_electron30.64
Forward intensity I(0) i0115810000.00
Molecular weight molecular_weight85624.0 kDa
Excluded volume excluded_volume107310 ų
Envelope volume envelope_volume134440 ų
Hydration-shell volume shell_volume37311 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg36.95
Envelope Rg envelope_rg30.41
Shape Rg shape_rg30.60
Total Rg total_rg31.30
Total atoms total_atoms5975
Residues n_residues774
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 dmax102.5
Rg (real space) rg_real31.28
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1580e+08
I(0) uncertainty (real space) i0_real_error1.7310e+06
Rg (reciprocal space) rg_reciprocal31.28
I(0) (reciprocal space) i0_reciprocal115800000.0000
Solution quality estimate total_estimate0.6882
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24650000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.966; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3ijob_
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_idd3ijoe_
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_idd3ijoh_
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 (6 domains)

Domain ID domain_id3ijoB01
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_id3ijoB02
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_id3ijoE01
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_id3ijoE02
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_id3ijoH01
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_id3ijoH02
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 (1)

9. Files and Curves (10)