› 3h6t

X-ray diffraction
2.25Å resolution

Crystal structure of the iGluR2 ligand-binding core (S1S2J-N754S) in complex with glutamate and cyclothiazide at 2.25 A resolution

Released:
DOI: 10.2210/pdb3h6t/pdb
PDB entry 3h6t coloured by chain, front view.
PDB entry 3h6t coloured by chain, side view.
PDB entry 3h6t coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Distinct structural features of cyclothiazide are responsible for effects on peak current amplitude and desensitization kinetics at iGluR2.
Hald H, Ahring PK, Timmermann DB, Liljefors T, Gajhede M, Kastrup JS
J Mol Biol 391 906-17 (2009)
PMID: 19591837

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
Molecule details ›
Chains: A, B, C
Length: 263 amino acids
Theoretical weight: 29.19 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

7 bound ligands:
Ligand GLU 3 x GLU
Ligand CYZ 3 x CYZ
Ligand ZN 10 x ZN
Ligand GOL 9 x GOL
Ligand ACT 2 x ACT
Ligand DMS 1 x DMS
Ligand CAC 1 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21212
Unit cell:
a: 114.486Å b: 163.136Å c: 47.354Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.228
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Functional insight into development of positive allosteric modulators of AMPA receptors.
Weeks et al. (2014)
1 more