› 1p1n

X-ray diffraction
1.6Å resolution

GluR2 Ligand Binding Core (S1S2J) Mutant L650T in Complex with Kainate

Released:
DOI: 10.2210/pdb1p1n/pdb
PDB 1p1n coloured by chain and viewed from the front.
PDB 1p1n coloured by chain and viewed from the side.
PDB 1p1n coloured by chain and viewed from the top.
Source organism: Rattus norvegicus
Primary publication:
Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.
Armstrong N, Mayer M, Gouaux E
Proc Natl Acad Sci U S A 100 5736-41 (2003)
PMID: 12730367

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.21 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P19491 (Residues: 413-527, 653-796; Coverage: 30%)
Gene names: Glur2, Gria2
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

1 bound ligand:
Ligand KAI 1 x KAI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 62.386Å b: 88.741Å c: 48.151Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.274 0.235 0.252
Expression system: Escherichia coli BL21

Quick links

Citations

20 review citations

Structural Dynamics of Glutamate Signaling Systems by smFRET.
Durham et al. (2020)
19 more

3 mentions without citation

Molecular crowding enhances native state stability and refolding rates of globular proteins.
Cheung et al. (2005)
2 more