4f3b

Glutamate bound to the D655A mutant of the ligand binding domain of GluA3

Method: X-RAY DIFFRACTION Dmax: 63.9 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 417–530 Chain A; UniProt 658–799 Mutation:D655A GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;14-15% PEG 8K, 0.1 M sodium cacodylate, 0.1-0.15 M zinc acetate, 0.25 M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.82 Å R-free 0.238

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 38 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 1–114; UniProt 417–530 Author chain A; PDBConstruct 117–258; UniProt 658–799

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 4f3b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4f3b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4f3b
Deposition date deposition_date2012-05-09
Structure title titleGlutamate bound to the D655A mutant of the ligand binding domain of GluA3
Keywords keywords;glutamate receptor, GluA3, GluR3, AMPA receptor, S1S2, LBD, neurotransmitter receptor, glutamate, TRANSPORT PROTEIN-SUBSTRATE complex ;; TRANSPORT PROTEIN/SUBSTRATE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.81
Radius of gyration Rg (electron density) rg_electron18.72
Forward intensity I(0) i014542100.00
Molecular weight molecular_weight29169.0 kDa
Excluded volume excluded_volume36789 ų
Envelope volume envelope_volume42714 ų
Hydration-shell volume shell_volume19050 ų
Envelope diameter envelope_diameter67.1
Shell Rg shell_rg24.90
Envelope Rg envelope_rg19.03
Shape Rg shape_rg18.68
Total Rg total_rg19.74
Total atoms total_atoms2042
Residues n_residues258
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 dmax63.9
Rg (real space) rg_real19.71
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.4540e+07
I(0) uncertainty (real space) i0_real_error1.9190e+05
Rg (reciprocal space) rg_reciprocal19.73
I(0) (reciprocal space) i0_reciprocal14540000.0000
Solution quality estimate total_estimate0.8139
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3145000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4f3ba_
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_id4f3bA01
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_id4f3bA02
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)