6zyu

Structure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM549

Method: X-RAY DIFFRACTION Dmax: 102.1 Å Quality: GOOD

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

Glutamate receptor 2,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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–797 Mutation:L483Y,N754S ZN ZINC ION × 4 CAC CACODYLATE ION × 2 ACT ACETATE ION × 4 GLU GLUTAMIC ACID × 2 QSZ (4~{S})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 QSW (4~{R})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 GOL GLYCEROL × 6 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;299 K;Zinc acetate, polyethylene glycol 4000, cacodylate Resolution 1.90 Å R-free 0.187
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–797 Chain C; UniProt 413–527 Chain C; UniProt 653–797 Mutation:L483Y,N754S ZN ZINC ION × 6 ACT ACETATE ION × 3 GLU GLUTAMIC ACID × 2 QSZ (4~{S})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 QSW (4~{R})-4-cyclopropyl-7-fluoranyl-3,4-dihydro-2~{H}-thiochromene 1,1-dioxide × 2 GOL GLYCEROL × 3 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;299 K;Zinc acetate, polyethylene glycol 4000, cacodylate Resolution 1.90 Å R-free 0.187

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 481 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 A; PDBConstruct 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–264; UniProt 653–797 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–264; UniProt 653–797 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; PDBConstruct 120–264; UniProt 653–797

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 6zyu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6zyu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6zyu
Deposition date deposition_date2020-08-03
Structure title titleStructure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM549
Keywords keywords;GLUA2-LBD, GLUA2-S1S2J, AMPA RECEPTOR, LIGAND-BINDING DOMAIN, POSITIVE ALLOSTERIC MODULATOR, MEMBRANE PROTEIN, L483Y, N754S, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.37
Radius of gyration Rg (electron density) rg_electron30.72
Forward intensity I(0) i0128145000.00
Molecular weight molecular_weight90189.0 kDa
Excluded volume excluded_volume113060 ų
Envelope volume envelope_volume143390 ų
Hydration-shell volume shell_volume39115 ų
Envelope diameter envelope_diameter108.8
Shell Rg shell_rg37.40
Envelope Rg envelope_rg30.80
Shape Rg shape_rg30.68
Total Rg total_rg31.43
Total atoms total_atoms6290
Residues n_residues787
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 dmax102.1
Rg (real space) rg_real31.38
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.2810e+08
I(0) uncertainty (real space) i0_real_error1.8870e+06
Rg (reciprocal space) rg_reciprocal31.38
I(0) (reciprocal space) i0_reciprocal128100000.0000
Solution quality estimate total_estimate0.8937
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28390000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6zyuA01
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_id6zyuB01
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_id6zyuC01
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)