Structure analysis

Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix

X-ray diffraction
2.35Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero pentamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero pentamer
Accessible surface area: 7948.95 Å2
Buried surface area: 7434.31 Å2
Dissociation area: 1,216.08 Å2
Dissociation energy (ΔGdiss): 13.22 kcal/mol
Dissociation entropy (TΔSdiss): 9.68 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-149586
Assembly 2
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Multimeric state: hetero pentamer
Accessible surface area: 8659.79 Å2
Buried surface area: 7244.58 Å2
Dissociation area: 1,104.3 Å2
Dissociation energy (ΔGdiss): 12.98 kcal/mol
Dissociation entropy (TΔSdiss): 9.76 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-149586

Macromolecules

Chains: A, B, C, D, E, F, G, H
Length: 40 amino acids
Theoretical weight: 5.13 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P22303 (Residues: 575-614; Coverage: 7%)
Gene name: ACHE
Pfam: Acetylcholinesterase tetramerisation domain
InterPro: Acetylcholinesterase, tetramerisation domain

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Chains: I, J
Length: 15 amino acids
Theoretical weight: 1.68 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y215 (Residues: 53-67; Coverage: 4%)
Gene name: COLQ

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