3p3w

Structure of a dimeric GluA3 N-terminal domain (NTD) at 4.2 A resolution

Method: X-RAY DIFFRACTION Dmax: 134.5 Å Quality: GOOD

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

Glutamate receptor 3

Rattus norvegicus

UniProt P19492

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 23–403 Chain C; UniProt 23–403 Fragment:N-terminal domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.7;293 K;200mM ammonium phosphate, 20% PEG3350, pH 4.7, VAPOR DIFFUSION, temperature 293K Resolution 4.20 Å R-free 0.338
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 23–403 Chain D; UniProt 23–403 Fragment:N-terminal domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.7;293 K;200mM ammonium phosphate, 20% PEG3350, pH 4.7, VAPOR DIFFUSION, temperature 293K Resolution 4.20 Å R-free 0.338

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.

32 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA3_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–381; UniProt 23–403 Author chain B; PDBConstruct 1–381; UniProt 23–403 Author chain C; PDBConstruct 1–381; UniProt 23–403 Author chain D; PDBConstruct 1–381; UniProt 23–403

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 3p3w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3p3w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3p3w
Deposition date deposition_date2010-10-05
Structure title titleStructure of a dimeric GluA3 N-terminal domain (NTD) at 4.2 A resolution
Keywords keywordsPeriplasmatic binding protein, 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_guinier39.84
Radius of gyration Rg (electron density) rg_electron39.34
Forward intensity I(0) i0401947000.00
Molecular weight molecular_weight162710.0 kDa
Excluded volume excluded_volume203060 ų
Envelope volume envelope_volume281560 ų
Hydration-shell volume shell_volume60063 ų
Envelope diameter envelope_diameter139.1
Shell Rg shell_rg44.60
Envelope Rg envelope_rg38.65
Shape Rg shape_rg39.36
Total Rg total_rg39.60
Total atoms total_atoms11484
Residues n_residues1482
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 dmax134.5
Rg (real space) rg_real39.88
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real4.0190e+08
I(0) uncertainty (real space) i0_real_error7.3740e+06
Rg (reciprocal space) rg_reciprocal39.86
I(0) (reciprocal space) i0_reciprocal401900000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.173
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha130600000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.789

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)