› 5cbs

X-ray diffraction
1.8Å resolution

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution

Released:
DOI: 10.2210/pdb5cbs/pdb
PDB entry 5cbs coloured by chain, front view.
PDB entry 5cbs coloured by chain, side view.
PDB entry 5cbs coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Studies on Aryl-Substituted Phenylalanines: Synthesis, Activity, and Different Binding Modes at AMPA Receptors.
Szymanska E, Frydenvang K, Pickering DS, Krintel C, Nielsen B, Kooshki A, Zachariassen LG, Olsen L, Kastrup JS, Johansen TN
J Med Chem 59 448-61 (2016)
PMID: 26653877

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: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 29.28 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19491 (Residues: 413-527, 653-797; Coverage: 30%)
Gene names: GluA2, Glur2, Gria2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

5 bound ligands:
Ligand E42 4 x E42
Ligand SO4 10 x SO4
Ligand EDO 14 x EDO
Ligand GOL 4 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 61.468Å b: 92.202Å c: 197.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.167 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.
Chałupnik et al. (2023)
5 other articles

1 mention without citation

Aryl- and heteroaryl-substituted phenylalanines as AMPA receptor ligands.
Szymańska et al. (2017)