› 3o2j

X-ray diffraction
1.95Å resolution

Structure of the GluA2 NTD-dimer interface mutant, N54A

Released:
DOI: 10.2210/pdb3o2j/pdb
PDB entry 3o2j coloured by chain, front view.
PDB entry 3o2j coloured by chain, side view.
PDB entry 3o2j coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.
Rossmann M, Sukumaran M, Penn AC, Veprintsev DB, Babu MM, Greger IH
EMBO J 30 959-71 (2011)
PMID: 21317873

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-148607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 43.96 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: P19491 (Residues: 22-400; Coverage: 44%)
Gene names: GluA2, Glur2, Gria2
Sequence domains: Receptor family ligand binding region
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 82.33Å b: 92.58Å c: 102.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.247
Expression system: Homo sapiens

Quick links

Citations

25 review citations

Synaptic AMPA receptor composition in development, plasticity and disease.
Henley et al. (2016)
24 more

1 mention without citation

Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.
Rossmann et al. (2011)