› 4dld

X-ray diffraction
2Å resolution

Crystal structure of the GluK1 ligand-binding domain (S1S2) in complex with the antagonist (S)-2-amino-3-(2-(2-carboxyethyl)-5-chloro-4-nitrophenyl)propionic acid at 2.0 A resolution

Released:
DOI: 10.2210/pdb4dld/pdb
PDB entry 4dld coloured by chain, front view.
PDB entry 4dld coloured by chain, side view.
PDB entry 4dld coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structural and pharmacological characterization of phenylalanine-based AMPA receptor antagonists at kainate receptors.
Venskutonytė R, Frydenvang K, Valadés EA, Szymańska E, Johansen TN, Kastrup JS, Pickering DS
ChemMedChem 7 1793-8 (2012)
PMID: 22407805

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-149794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor ionotropic, kainate 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 29.11 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22756 (Residues: 445-559, 682-820; Coverage: 28%)
Gene names: Glur5, Grik1
Sequence domains:
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

4 bound ligands:
Ligand TZG 2 x TZG
Ligand CL 1 x CL
Ligand SO4 1 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P41212
Unit cell:
a: 69.32Å b: 69.32Å c: 234.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.246
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.
Chałupnik et al. (2023)
6 other articles

6 mentions without citation

Ligand pose and orientational sampling in molecular docking.
Coleman et al. (2013)
5 more