› 3tza

X-ray diffraction
1.9Å resolution

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid at 1.9A resolution

Released:
DOI: 10.2210/pdb3tza/pdb
PDB entry 3tza coloured by chain, front view.
PDB entry 3tza coloured by chain, side view.
PDB entry 3tza coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
A new phenylalanine derivative acts as an antagonist at the AMPA receptor GluA2 and introduces partial domain closure: synthesis, resolution, pharmacology, and crystal structure.
Szymańska E, Frydenvang K, Contreras-Sanz A, Pickering DS, Frola E, Serafimoska Z, Nielsen B, Kastrup JS, Johansen TN
J Med Chem 54 7289-98 (2011)
PMID: 21923187

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
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.22 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19491 (Residues: 413-527, 653-796; Coverage: 30%)
Gene names: GluA2, Glur2, Gria2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand TZG 2 x TZG
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 48.722Å b: 61.835Å c: 92.921Å
α: 90° β: 94.09° γ: 90°
R-values:
R R work R free
0.174 0.172 0.23
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Heterocycles as nonclassical bioisosteres of α-amino acids.
Poulie et al. (2013)
1 more