› 4igt

X-ray diffraction
1.24Å resolution

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist ZA302 at 1.24A resolution

Released:
DOI: 10.2210/pdb4igt/pdb
PDB entry 4igt coloured by chain, front view.
PDB entry 4igt coloured by chain, side view.
PDB entry 4igt coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Chemoenzymatic synthesis of new 2,4-syn-functionalized (S)-glutamate analogues and structure-activity relationship studies at ionotropic glutamate receptors and excitatory amino acid transporters.
Assaf Z, Larsen AP, Venskutonytė R, Han L, Abrahamsen B, Nielsen B, Gajhede M, Kastrup JS, Jensen AA, Pickering DS, Frydenvang K, Gefflaut T, Bunch L
J Med Chem 56 1614-28 (2013)
PMID: 23414088

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 Chain: A
Molecule details ›
Chain: A
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

4 bound ligands:
Ligand 3ZA 1 x 3ZA
Ligand SO4 3 x SO4
Ligand LI 1 x LI
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21212
Unit cell:
a: 59.613Å b: 95.641Å c: 48.455Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.136 0.155
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Enzymatic asymmetric synthesis of chiral amino acids.
Xue et al. (2018)
1 more

2 mentions without citation

Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.
Hansen et al. (2021)
1 more