1sd3

Crystal structure of the GLUR6 ligand binding core in complex with 2S,4R-4-methylglutamate at 1.8 Angstrom resolution

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: GOOD

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

Glutamate receptor, ionotropic kainate 2

Rattus norvegicus

UniProt P42260

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 429–544 Chain A; UniProt 667–806 Chain B; UniProt 429–544 Chain B; UniProt 667–806 Fragment:residues 1-259 SYM 2S,4R-4-METHYLGLUTAMATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.9;293 K;14% PEG 3350, 10mM malonate, 10mM BME, 20mM NaCl, 2mM Citrate, 1mM EDTA, 4.5mM 2S,4R-4-methylglutamate, pH 4.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.256

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.

91 other PDB entries and 106 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIK2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–117; UniProt 429–544 Author chain A; PDBConstruct 120–259; UniProt 667–806 Author chain B; PDBConstruct 2–117; UniProt 429–544 Author chain B; PDBConstruct 120–259; UniProt 667–806

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 1sd3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sd3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sd3
Deposition date deposition_date2004-02-12
Structure title titleCrystal structure of the GLUR6 ligand binding core in complex with 2S,4R-4-methylglutamate at 1.8 Angstrom 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_guinier25.60
Radius of gyration Rg (electron density) rg_electron24.50
Forward intensity I(0) i052440700.00
Molecular weight molecular_weight57554.0 kDa
Excluded volume excluded_volume72654 ų
Envelope volume envelope_volume88028 ų
Hydration-shell volume shell_volume29739 ų
Envelope diameter envelope_diameter88.7
Shell Rg shell_rg32.08
Envelope Rg envelope_rg24.56
Shape Rg shape_rg24.50
Total Rg total_rg25.36
Total atoms total_atoms4046
Residues n_residues502
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 dmax85.8
Rg (real space) rg_real25.54
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real5.2440e+07
I(0) uncertainty (real space) i0_real_error8.0940e+05
Rg (reciprocal space) rg_reciprocal25.56
I(0) (reciprocal space) i0_reciprocal52440000.0000
Solution quality estimate total_estimate0.8054
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.4
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.294
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28250000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1sd3a_
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.94.1.0 — automated matches
Domain ID domain_idd1sd3b_
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.94.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id1sd3A01
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_id1sd3A02
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_id1sd3B01
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_id1sd3B02
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)