2xxt

Crystal structure of the GluK2 (GluR6) wild-type LBD dimer in complex with kainate

Method: X-RAY DIFFRACTION Dmax: 84.8 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 × 2 PDB declaration: dimeric(2) 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:LIGAND BINDING DOMAIN, RESIDUES 429-544,667-806 KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2 NA SODIUM ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;VAPOR DIFFUSION, HANGING DROP 23% PEG 4000, 9% PROPAN-2-OL, 80MM SODIUM ACETATE. Resolution 1.90 Å R-free 0.209

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 2xxt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2xxt
Deposition date deposition_date2010-11-12
Structure title titleCrystal structure of the GluK2 (GluR6) wild-type LBD dimer in complex with kainate
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.95
Radius of gyration Rg (electron density) rg_electron23.66
Forward intensity I(0) i050166400.00
Molecular weight molecular_weight56885.0 kDa
Excluded volume excluded_volume71980 ų
Envelope volume envelope_volume85481 ų
Hydration-shell volume shell_volume29332 ų
Envelope diameter envelope_diameter89.6
Shell Rg shell_rg31.51
Envelope Rg envelope_rg23.88
Shape Rg shape_rg23.66
Total Rg total_rg24.57
Total atoms total_atoms3997
Residues n_residues496
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 dmax84.8
Rg (real space) rg_real24.79
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real5.0170e+07
I(0) uncertainty (real space) i0_real_error7.9600e+05
Rg (reciprocal space) rg_reciprocal24.83
I(0) (reciprocal space) i0_reciprocal50170000.0000
Solution quality estimate total_estimate0.7958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary33.6
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.516
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15650000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2xxta_
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_idd2xxtb_
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_id2xxtA01
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_id2xxtA02
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_id2xxtB01
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_id2xxtB02
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)