2al4

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH quisqualate and CX614.

Method: X-RAY DIFFRACTION Dmax: 160.9 Å Quality: REASONABLE

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–796 Chain B; UniProt 413–527 Chain B; UniProt 653–796 Chain F; UniProt 413–527 Chain F; UniProt 653–796 Fragment:ligand binding core (S1S2J) Mutation:The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. ZN ZINC ION × 5 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 3 CX6 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;10-14% PEG8000, 0.1-0.15 M Zinc acetate, 0.1 M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.70 Å R-free 0.223
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 413–527 Chain C; UniProt 653–796 Chain D; UniProt 413–527 Chain D; UniProt 653–796 Chain E; UniProt 413–527 Chain E; UniProt 653–796 Fragment:ligand binding core (S1S2J) Mutation:The native GluR2 is a membrane protein. Transmembrane regions were genetically removed and replaced with a Gly-Thr linker. ZN ZINC ION × 5 QUS (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID × 3 CX6 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;10-14% PEG8000, 0.1-0.15 M Zinc acetate, 0.1 M sodium acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.70 Å R-free 0.223

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 GLR2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–263; UniProt 653–796 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–263; UniProt 653–796 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; PDBConstruct 120–263; UniProt 653–796 Author chain D; PDBConstruct 3–117; UniProt 413–527 Author chain D; PDBConstruct 120–263; UniProt 653–796 Author chain E; PDBConstruct 3–117; UniProt 413–527 Author chain E; PDBConstruct 120–263; UniProt 653–796 Author chain F; PDBConstruct 3–117; UniProt 413–527 Author chain F; PDBConstruct 120–263; UniProt 653–796

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 2al4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2al4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2al4
Deposition date deposition_date2005-08-04
Structure title titleCRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH quisqualate and CX614.
Keywords keywordsIONOTROPIC GLUTAMATE RECEPTOR, GLUR2, LIGAND BINDING CORE, S1S2, quisqualate, CX614, modulator, 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_guinier50.64
Radius of gyration Rg (electron density) rg_electron51.19
Forward intensity I(0) i0418947000.00
Molecular weight molecular_weight169950.0 kDa
Excluded volume excluded_volume212830 ų
Envelope volume envelope_volume291300 ų
Hydration-shell volume shell_volume52146 ų
Envelope diameter envelope_diameter177.6
Shell Rg shell_rg47.55
Envelope Rg envelope_rg50.36
Shape Rg shape_rg51.20
Total Rg total_rg51.00
Total atoms total_atoms11892
Residues n_residues1550
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 dmax160.9
Rg (real space) rg_real51.12
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real4.1890e+08
I(0) uncertainty (real space) i0_real_error7.8220e+06
Rg (reciprocal space) rg_reciprocal50.21
I(0) (reciprocal space) i0_reciprocal418400000.0000
Solution quality estimate total_estimate0.7455
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.529
Kurtosis Kurtosis kurtosis-0.620
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49830000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.704; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.577; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2al4a_
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_idd2al4b_
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_idd2al4c_
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_idd2al4d_
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_idd2al4e_
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_idd2al4f_
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 (12 domains)

Domain ID domain_id2al4A01
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_id2al4A02
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_id2al4B01
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_id2al4B02
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_id2al4C01
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_id2al4C02
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_id2al4D01
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_id2al4D02
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_id2al4E01
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_id2al4E02
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_id2al4F01
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_id2al4F02
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)