3bft

Structure of the ligand-binding core of GluR2 in complex with the agonist (S)-TDPA at 2.25 A resolution

Method: X-RAY DIFFRACTION Dmax: 126.1 Å Quality: GOOD

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 A; UniProt 653–796 Chain C; UniProt 413–527 Chain C; UniProt 653–796 Fragment:residues 1-263 S2P (2S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2 ZN ZINC ION × 2 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;279 K;PEG 2000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 2.27 Å R-free 0.250
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–796 Fragment:residues 1-263 S2P (2S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propanoic acid × 2 ZN ZINC ION × 6 NA SODIUM ION × 2 CAC CACODYLATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;279 K;PEG 2000, cacodylate, zinc acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K Resolution 2.27 Å R-free 0.250

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 A; PDBConstruct 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–263; UniProt 653–796 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–263; UniProt 653–796 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; 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 3bft

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3bft
Deposition date deposition_date2007-11-23
Structure title titleStructure of the ligand-binding core of GluR2 in complex with the agonist (S)-TDPA at 2.25 A resolution
Keywords keywords;AMPA receptor, GluR2, ligand-binding core, agonist, (S)-TDPA, Cell junction, Endoplasmic reticulum, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, Membrane, Palmitate, Phosphoprotein, Postsynaptic cell membrane, 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_guinier37.09
Radius of gyration Rg (electron density) rg_electron37.21
Forward intensity I(0) i0117199000.00
Molecular weight molecular_weight87805.0 kDa
Excluded volume excluded_volume110300 ų
Envelope volume envelope_volume148390 ų
Hydration-shell volume shell_volume36287 ų
Envelope diameter envelope_diameter128.6
Shell Rg shell_rg39.56
Envelope Rg envelope_rg36.94
Shape Rg shape_rg37.14
Total Rg total_rg37.62
Total atoms total_atoms6127
Residues n_residues777
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 dmax126.1
Rg (real space) rg_real37.52
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.1720e+08
I(0) uncertainty (real space) i0_real_error2.0870e+06
Rg (reciprocal space) rg_reciprocal37.26
I(0) (reciprocal space) i0_reciprocal117200000.0000
Solution quality estimate total_estimate0.7861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.512
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13700000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.648; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.570; Smooth: 0.700

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3bfta_
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_idd3bftb_
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_idd3bftc_
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_id3bftA01
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_id3bftA02
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_id3bftB01
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_id3bftB02
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_id3bftC01
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_id3bftC02
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)