3h06

Crystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282

Method: X-RAY DIFFRACTION Dmax: 144.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 414–527 Chain G; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
10 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 414–527 Chain E; UniProt 653–794 Chain P; UniProt 414–527 Chain P; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
11 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 414–527 Chain G; UniProt 653–794 Chain J; UniProt 414–527 Chain J; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
12 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 414–527 Chain H; UniProt 653–794 Chain L; UniProt 414–527 Chain L; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 414–527 Chain B; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 414–527 Chain E; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain H; UniProt 414–527 Chain H; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain J; UniProt 414–527 Chain J; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain L; UniProt 414–527 Chain L; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
7 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain N; UniProt 414–527 Chain N; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
8 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain P; UniProt 414–527 Chain P; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295
9 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 N; UniProt 414–527 Chain N; UniProt 653–794 Fragment:UNP residues 414-527, 652-794 VBP 4-({3-[(2R)-2-amino-2-carboxyethyl]-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl}methyl)benzoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15-17% PEG8K, 0.2 M Na acetate, 0.2 M Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.80 Å R-free 0.295

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 471 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 G; PDBConstruct 1–114; UniProt 414–527 Author chain G; PDBConstruct 117–258; UniProt 653–794 Author chain H; PDBConstruct 1–114; UniProt 414–527 Author chain H; PDBConstruct 117–258; UniProt 653–794 Author chain J; PDBConstruct 1–114; UniProt 414–527 Author chain J; PDBConstruct 117–258; UniProt 653–794 Author chain L; PDBConstruct 1–114; UniProt 414–527 Author chain L; PDBConstruct 117–258; UniProt 653–794 Author chain N; PDBConstruct 1–114; UniProt 414–527 Author chain N; PDBConstruct 117–258; UniProt 653–794 Author chain P; PDBConstruct 1–114; UniProt 414–527 Author chain P; 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 3h06

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h06
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h06
Deposition date deposition_date2009-04-08
Structure title titleCrystal structure of the binding domain of the AMPA subunit GluR2 bound to the willardiine antagonist, UBP282
Keywords keywordsglutamate receptor, glur2, AMPA receptor, neurotransmitter receptor, S1S2, 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_guinier44.76
Radius of gyration Rg (electron density) rg_electron44.34
Forward intensity I(0) i0759626000.00
Molecular weight molecular_weight232040.0 kDa
Excluded volume excluded_volume292490 ų
Envelope volume envelope_volume407730 ų
Hydration-shell volume shell_volume75724 ų
Envelope diameter envelope_diameter154.3
Shell Rg shell_rg50.42
Envelope Rg envelope_rg43.09
Shape Rg shape_rg44.33
Total Rg total_rg44.63
Total atoms total_atoms16272
Residues n_residues2056
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 dmax144.4
Rg (real space) rg_real44.60
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real7.5960e+08
I(0) uncertainty (real space) i0_real_error1.3490e+07
Rg (reciprocal space) rg_reciprocal44.76
I(0) (reciprocal space) i0_reciprocal759800000.0000
Solution quality estimate total_estimate0.8953
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.8
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.515
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha127900000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3h06b_
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_idd3h06e_
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_idd3h06g_
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_idd3h06h_
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_idd3h06j_
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_idd3h06l_
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_idd3h06n_
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_idd3h06p_
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 (16 domains)

Domain ID domain_id3h06B01
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_id3h06B02
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_id3h06E01
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_id3h06E02
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_id3h06G01
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_id3h06G02
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_id3h06H01
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_id3h06H02
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_id3h06J01
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_id3h06J02
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_id3h06L01
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_id3h06L02
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_id3h06N01
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_id3h06N02
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_id3h06P01
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_id3h06P02
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)