3pd9

X-ray structure of the ligand-binding core of GluA2 in complex with (R)-5-HPCA at 2.1 A resolution

Method: X-RAY DIFFRACTION Dmax: 80.3 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–795 Chain B; UniProt 413–527 Chain B; UniProt 653–795 Fragment:UNP residues 413-527, 653-795 HA5 (5R)-3-hydroxy-4,5,6,7-tetrahydroisoxazolo[5,4-c]pyridine-5-carboxylic acid × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 5 CL CHLORIDE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;280 K;PEG4000, ammonium sulfate, acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 280K Resolution 2.10 Å R-free 0.233

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 482 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 1–115; UniProt 413–527 Author chain A; PDBConstruct 118–260; UniProt 653–795 Author chain B; PDBConstruct 1–115; UniProt 413–527 Author chain B; PDBConstruct 118–260; UniProt 653–795

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 3pd9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3pd9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3pd9
Deposition date deposition_date2010-10-22
Structure title titleX-ray structure of the ligand-binding core of GluA2 in complex with (R)-5-HPCA at 2.1 A resolution
Keywords keywordsionotropic glutamate receptor GluA2, ligand-binding core, agonist complex, 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_guinier25.28
Radius of gyration Rg (electron density) rg_electron24.06
Forward intensity I(0) i057094100.00
Molecular weight molecular_weight59093.0 kDa
Excluded volume excluded_volume74156 ų
Envelope volume envelope_volume89454 ų
Hydration-shell volume shell_volume30097 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg32.13
Envelope Rg envelope_rg24.18
Shape Rg shape_rg24.01
Total Rg total_rg25.13
Total atoms total_atoms4128
Residues n_residues518
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 dmax80.3
Rg (real space) rg_real25.15
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.7090e+07
I(0) uncertainty (real space) i0_real_error7.8640e+05
Rg (reciprocal space) rg_reciprocal25.19
I(0) (reciprocal space) i0_reciprocal57100000.0000
Solution quality estimate total_estimate0.8987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.1
Skewness Skewness skewness0.139
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14030000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3pd9a_
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_idd3pd9b_
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 (4 domains)

Domain ID domain_id3pd9A01
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_id3pd9A02
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_id3pd9B01
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_id3pd9B02
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 (3)

9. Files and Curves (10)