2gfe

Crystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution

Method: X-RAY DIFFRACTION Dmax: 101.0 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 C; UniProt 413–527 Chain C; UniProt 653–795 Mutation:A476E S673D ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.54 Å R-free 0.227
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–795 Mutation:A476E S673D ZN ZINC ION × 2 GLU GLUTAMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.54 Å R-free 0.227
3 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) 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 Chain C; UniProt 413–527 Chain C; UniProt 653–795 Mutation:A476E S673D ZN ZINC ION × 5 GLU GLUTAMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.54 Å R-free 0.227
4 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 Mutation:A476E S673D ZN ZINC ION × 3 GLU GLUTAMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;1 to 1 mixture of: Reservoir: 14% PEG 8K; 0.1M Na Acetate; 0.1 M Zn Acetate. Protein: 10 mg/ml 0.01 M Na HEPES pH 7.0; 0.02 M NaCl; 0.01 M Na Glutamate; 0.001 M EDTA, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.54 Å R-free 0.227

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 479 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 120–262; UniProt 653–795 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–262; UniProt 653–795 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; PDBConstruct 120–262; 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 2gfe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gfe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gfe
Deposition date deposition_date2006-03-21
Structure title titleCrystal structure of the GluR2 A476E S673D Ligand Binding Core Mutant at 1.54 Angstroms Resolution
Keywords keywordsMEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.34
Radius of gyration Rg (electron density) rg_electron30.69
Forward intensity I(0) i0120759000.00
Molecular weight molecular_weight87923.0 kDa
Excluded volume excluded_volume110530 ų
Envelope volume envelope_volume140090 ų
Hydration-shell volume shell_volume38565 ų
Envelope diameter envelope_diameter108.1
Shell Rg shell_rg37.16
Envelope Rg envelope_rg30.58
Shape Rg shape_rg30.65
Total Rg total_rg31.43
Total atoms total_atoms6146
Residues n_residues780
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 dmax101.0
Rg (real space) rg_real31.35
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.2080e+08
I(0) uncertainty (real space) i0_real_error2.2250e+06
Rg (reciprocal space) rg_reciprocal31.35
I(0) (reciprocal space) i0_reciprocal120800000.0000
Solution quality estimate total_estimate0.8715
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.6
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.374
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26030000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.604

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2gfea1
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_idd2gfea2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gfeb1
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_idd2gfeb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gfec1
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_idd2gfec2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id2gfeA01
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_id2gfeA02
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_id2gfeB01
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_id2gfeB02
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_id2gfeC01
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_id2gfeC02
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)