› 5ybg

X-ray diffraction
1.52Å resolution

Crystal structure of the GluA2o LBD in complex with glutamate and LY451395

Released:
DOI: 10.2210/pdb5ybg/pdb
PDB 5ybg coloured by chain and viewed from the front.
PDB 5ybg coloured by chain and viewed from the side.
PDB 5ybg coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry authors: Sogabe S, Igaki S, Hirokawa A, Zama Y, Lane W, Snell G

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 263 amino acids
Theoretical weight: 29.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42262 (Residues: 413-527, 653-796; Coverage: 30%)
Gene names: GLUR2, GRIA2
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

5 bound ligands:
Ligand GLU 6 x GLU
Ligand 8SO 3 x 8SO
Ligand ZN 10 x ZN
Ligand ACT 5 x ACT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21
Unit cell:
a: 113.724Å b: 161.913Å c: 46.964Å
α: 90° β: 89.97° γ: 90°
R-values:
R R work R free
0.204 0.202 0.233
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

TAK-137, an AMPA-R potentiator with little agonistic effect, has a wide therapeutic window.
Kunugi et al. (2019)
3 more