› 4gxs

X-ray diffraction
1.96Å resolution

Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin

Released:
DOI: 10.2210/pdb4gxs/pdb
PDB entry 4gxs coloured by chain, front view.
PDB entry 4gxs coloured by chain, side view.
PDB entry 4gxs coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The structure of (-)-kaitocephalin bound to the ligand binding domain of the (S)-α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)/glutamate receptor, GluA2.
Ahmed AH, Hamada M, Shinada T, Ohfune Y, Weerasinghe L, Garner PP, Oswald RE
J Biol Chem 287 41007-13 (2012)
PMID: 23076153

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chains: B, D
Molecule details ›
Chains: B, D
Length: 258 amino acids
Theoretical weight: 28.84 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19491 (Residues: 414-527, 653-794; Coverage: 30%)
Gene names: GluA2, Glur2, Gria2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand 0YS 2 x 0YS
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21212
Unit cell:
a: 96.741Å b: 121.466Å c: 48.899Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.225
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Spinal Cord Injury: Pathophysiology, Multimolecular Interactions, and Underlying Recovery Mechanisms.
Anjum et al. (2020)
3 other articles

1 mention without citation

The structure of (-)-kaitocephalin bound to the ligand binding domain of the (S)-α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)/glutamate receptor, GluA2.
Ahmed et al. (2012)