› 4o3c

X-ray diffraction
1.5Å resolution

Crystal structure of the GLUA2 ligand-binding domain in complex with L-aspartate at 1.50 A resolution

Released:
DOI: 10.2210/pdb4o3c/pdb
PDB entry 4o3c coloured by chain, front view.
PDB entry 4o3c coloured by chain, side view.
PDB entry 4o3c coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
L-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domain.
Krintel C, Frydenvang K, Ceravalls de Rabassa A, Kaern AM, Gajhede M, Pickering DS, Kastrup JS
FEBS J 281 2422-30 (2014)
PMID: 24673938

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

6 bound ligands:
Ligand ASP 1 x ASP
Ligand CL 1 x CL
Ligand GOL 1 x GOL
Ligand ACT 1 x ACT
Ligand LI 1 x LI
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21212
Unit cell:
a: 63.997Å b: 87.877Å c: 47.042Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.127 0.158
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Functional Validation of Heteromeric Kainate Receptor Models.
Paramo et al. (2017)
3 more

1 mention without citation

L-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domain.
Krintel et al. (2014)