3bki

Crystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms

Method: X-RAY DIFFRACTION Dmax: 146.9 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain P; UniProt 413–527 Chain P; UniProt 653–796 Not recorded FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP Resolution 1.87 Å R-free 0.221
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–796 Not recorded FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP Resolution 1.87 Å R-free 0.221
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 413–527 Chain C; UniProt 653–796 Not recorded FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP Resolution 1.87 Å R-free 0.221
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 413–527 Chain D; UniProt 653–796 Not recorded FQX [1,2,5]oxadiazolo[3,4-g]quinoxaline-6,7(5H,8H)-dione 1-oxide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP Resolution 1.87 Å R-free 0.221

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 479 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 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 Author chain D; PDBConstruct 3–117; UniProt 413–527 Author chain D; PDBConstruct 120–263; UniProt 653–796 Author chain P; PDBConstruct 3–117; UniProt 413–527 Author chain P; 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 3bki

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3bki
Deposition date deposition_date2007-12-06
Structure title titleCrystal Structure of the GluR2 ligand binding core (S1S2J) in complex with FQX at 1.87 Angstroms
Keywords keywords;AMPA receptor, ANQX, quinoxaline-2, 3-diones, Alternative splicing, Cell junction, Endoplasmic reticulum, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, Membrane, Palmitate, Phosphoprotein, Postsynaptic cell membrane, RNA editing, Synapse, Transmembrane, Transport, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.79
Radius of gyration Rg (electron density) rg_electron41.26
Forward intensity I(0) i0197622000.00
Molecular weight molecular_weight115500.0 kDa
Excluded volume excluded_volume145440 ų
Envelope volume envelope_volume199440 ų
Hydration-shell volume shell_volume45219 ų
Envelope diameter envelope_diameter154.4
Shell Rg shell_rg40.61
Envelope Rg envelope_rg41.41
Shape Rg shape_rg41.24
Total Rg total_rg41.30
Total atoms total_atoms8100
Residues n_residues1028
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 dmax146.9
Rg (real space) rg_real43.14
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.9910e+08
I(0) uncertainty (real space) i0_real_error3.4900e+06
Rg (reciprocal space) rg_reciprocal40.79
I(0) (reciprocal space) i0_reciprocal197500000.0000
Solution quality estimate total_estimate0.5861
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.7
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis-0.065
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha1.8000
Highest regularization parameter α highest_alpha18910000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 0.858; Sysdev: 0.000; Positv: 1.000; Valcen: 0.601; Smooth: 0.259

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3bkib_
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_idd3bkic_
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_idd3bkid_
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_idd3bkip_
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 (8 domains)

Domain ID domain_id3bkiB01
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_id3bkiB02
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_id3bkiC01
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_id3bkiC02
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_id3bkiD01
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_id3bkiD02
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_id3bkiP01
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_id3bkiP02
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)