5jei

Crystal structure of the GluA2 LBD in complex with FW

Method: X-RAY DIFFRACTION Dmax: 67.0 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–797 Mutation:V154C,V154C FWD 2-AMINO-3-(5-FLUORO-2,4-DIOXO-3,4-DIHYDRO-2H-PYRIMIDIN-1-YL)-PROPIONIC ACID × 4 PO4 PHOSPHATE ION × 8 PG4 TETRAETHYLENE GLYCOL × 8 PEG DI(HYDROXYETHYL)ETHER × 12 TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL × 4 PG0 2-(2-METHOXYETHOXY)ETHANOL × 4 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 8 EDO 1,2-ETHANEDIOL × 4 NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;277 K;50.0 % v/v PEG 200, 200 mM Sodium Chloride, 100 mM Sodium/Potassium Phosphate pH 6.2 Resolution 1.23 Å R-free 0.147

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 3–117; UniProt 413–527 Author chain A; 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 5jei

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jei
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5jei
Deposition date deposition_date2016-04-18
Structure title titleCrystal structure of the GluA2 LBD in complex with FW
Keywords keywordstransport protein, ligand binding domain, glutamate receptor 2; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.86
Radius of gyration Rg (electron density) rg_electron18.75
Forward intensity I(0) i016610200.00
Molecular weight molecular_weight31042.0 kDa
Excluded volume excluded_volume39048 ų
Envelope volume envelope_volume45175 ų
Hydration-shell volume shell_volume19885 ų
Envelope diameter envelope_diameter66.0
Shell Rg shell_rg25.28
Envelope Rg envelope_rg19.15
Shape Rg shape_rg18.71
Total Rg total_rg19.81
Total atoms total_atoms4361
Residues n_residues264
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 dmax67.0
Rg (real space) rg_real19.76
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.6610e+07
I(0) uncertainty (real space) i0_real_error2.1360e+05
Rg (reciprocal space) rg_reciprocal19.77
I(0) (reciprocal space) i0_reciprocal16610000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3877000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5jeia1
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_idd5jeia2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5jeiA01
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_id5jeiA02
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)