› 2ojt

X-ray diffraction
1.95Å resolution

Structure and mechanism of kainate receptor modulation by anions

Released:
DOI: 10.2210/pdb2ojt/pdb
PDB entry 2ojt coloured by chain, front view.
PDB entry 2ojt coloured by chain, side view.
PDB entry 2ojt coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure and mechanism of kainate receptor modulation by anions.
Plested AJ, Mayer ML
Neuron 53 829-41 (2007)
PMID: 17359918

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor ionotropic, kainate 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 29.21 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22756 (Residues: 446-821; Coverage: 28%)
Gene names: Glur5, Grik1
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

3 bound ligands:
Ligand BR 2 x BR
Ligand 1PE 2 x 1PE
Ligand UBA 2 x UBA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 97.598Å b: 97.732Å c: 128.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.233
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Glutamate receptor ion channels: structure, regulation, and function.
Traynelis et al. (2010)
18 more

2 mentions without citation

Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.
Nayeem et al. (2013)
1 more