3en3

Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate

Method: X-RAY DIFFRACTION Dmax: 62.5 Å Quality: EXCELLENT

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

Glutamate receptor 4,Glutamate receptor

Rattus norvegicus

UniProt P19493

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 416–528 Chain A; UniProt 654–795 Fragment:ligand binding domain (UNP residues 416-528 and 654-958) KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;291 K;25.5% PEG 1500, 0.05M Na-Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.43 Å R-free 0.219
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 416–528 Chain A; UniProt 654–795 Fragment:ligand binding domain (UNP residues 416-528 and 654-958) KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;291 K;25.5% PEG 1500, 0.05M Na-Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.43 Å R-free 0.219

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.

25 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA4_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–113; UniProt 416–528 Author chain A; PDBConstruct 116–257; UniProt 654–795

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 3en3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3en3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3en3
Deposition date deposition_date2008-09-25
Structure title titleCrystal Structure of the GluR4 Ligand-Binding domain in complex with kainate
Keywords keywords;GluR4, AMPA receptor, ligand-gated ion channel, ligand-binding domain, Kainate, Cell junction, Cell membrane, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, 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_guinier19.84
Radius of gyration Rg (electron density) rg_electron18.79
Forward intensity I(0) i014083100.00
Molecular weight molecular_weight28916.0 kDa
Excluded volume excluded_volume36581 ų
Envelope volume envelope_volume43160 ų
Hydration-shell volume shell_volume19121 ų
Envelope diameter envelope_diameter63.6
Shell Rg shell_rg25.11
Envelope Rg envelope_rg19.12
Shape Rg shape_rg18.76
Total Rg total_rg19.84
Total atoms total_atoms2029
Residues n_residues257
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 dmax62.5
Rg (real space) rg_real19.73
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.4080e+07
I(0) uncertainty (real space) i0_real_error1.5950e+05
Rg (reciprocal space) rg_reciprocal19.75
I(0) (reciprocal space) i0_reciprocal14080000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3039000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3en3a_
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 (2 domains)

Domain ID domain_id3en3A01
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_id3en3A02
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)