Structure analysis

Crystal structure of the AMPA receptor GluA2/A4 N-terminal domain heterodimer

X-ray diffraction
2.5Å resolution
Source organism: Rattus norvegicus
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 30691.2 Å2
Buried surface area: 3502.04 Å2
Dissociation area: 1,317.41 Å2
Dissociation energy (ΔGdiss): 13.2 kcal/mol
Dissociation entropy (TΔSdiss): 13.65 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-148606
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 31490.1 Å2
Buried surface area: 3110.83 Å2
Dissociation area: 1,286.92 Å2
Dissociation energy (ΔGdiss): 6.27 kcal/mol
Dissociation entropy (TΔSdiss): 13.66 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-148606

Macromolecules

Chains: A, C
Length: 385 amino acids
Theoretical weight: 43.73 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: P19491 (Residues: 25-400; Coverage: 44%)
Gene names: GluA2, Glur2, Gria2
Pfam: Receptor family ligand binding region
InterPro:
CATH: Rossmann fold

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Chains: B, D
Length: 389 amino acids
Theoretical weight: 44.55 KDa
Source organism: Rattus norvegicus
Expression system: Homo sapiens
UniProt:
  • Canonical: P19493 (Residues: 22-401; Coverage: 43%)
Gene names: Glur4, Gria4
Pfam: Receptor family ligand binding region
InterPro:
CATH: Rossmann fold

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