1ftk

CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2I) IN COMPLEX WITH KAINATE AT 1.6 A RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 59.0 Å Quality: REASONABLE

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

GLUTAMATE RECEPTOR SUBUNIT 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 404–528 Chain A; UniProt 653–796 Fragment:LIGAND BINDING CORE, S1S2I KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;15% PEG 8000 50 mM potassium phosphate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.60 Å R-free 0.261

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 6–130; UniProt 404–528 Author chain A; PDBConstruct 136–279; 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 1ftk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ftk
Deposition date deposition_date2000-09-12
Structure title titleCRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2I) IN COMPLEX WITH KAINATE AT 1.6 A RESOLUTION
Keywords keywordsGluR2, S1S2, ligand binding domain, kainate, partial agonist, ionotropic glutamate receptor, 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_guinier19.31
Radius of gyration Rg (electron density) rg_electron18.13
Forward intensity I(0) i012808100.00
Molecular weight molecular_weight26921.0 kDa
Excluded volume excluded_volume33766 ų
Envelope volume envelope_volume38882 ų
Hydration-shell volume shell_volume17952 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg24.22
Envelope Rg envelope_rg18.46
Shape Rg shape_rg18.11
Total Rg total_rg19.11
Total atoms total_atoms1889
Residues n_residues250
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 dmax59.0
Rg (real space) rg_real19.39
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real1.2490e+07
I(0) uncertainty (real space) i0_real_error1.0890e+05
Rg (reciprocal space) rg_reciprocal19.24
I(0) (reciprocal space) i0_reciprocal12810000.0000
Solution quality estimate total_estimate0.6954
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha8.9420
Highest regularization parameter α highest_alpha2816000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 0.926; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.433

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ftka_
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 (2 domains)

Domain ID domain_id1ftkA01
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_id1ftkA02
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 (2)

9. Files and Curves (10)