Structure analysis

The cryo-EM structure of human ERAD retro-translocation complex

Electron Microscopy
3.61Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero decamer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero decamer
Accessible surface area: 262798.19 Å2
Buried surface area: 52020.59 Å2
Dissociation area: 4,121.98 Å2
Dissociation energy (ΔGdiss): 7.32 kcal/mol
Dissociation entropy (TΔSdiss): 57.29 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-232467

Macromolecules

Chains: W, X, Y, Z
Length: 226 amino acids
Theoretical weight: 26.48 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9BUN8 (Residues: 1-251; Coverage: 90%)
Gene names: DER1, DERL1, UNQ243/PRO276
Pfam: Der1-like family

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Chains: A, B, C, D, E, F
Length: 787 amino acids
Theoretical weight: 87.55 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P55072 (Residues: 21-806; Coverage: 98%)
Gene names: HEL-220, HEL-S-70, VCP
Pfam:

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