› 7y53

Electron Microscopy
3.61Å resolution

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

Released:
DOI: 10.2210/pdb7y53/pdb
PDB entry 7y53 coloured by chain, front view.
PDB entry 7y53 coloured by chain, side view.
PDB entry 7y53 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The cryo-EM structure of the human ERAD retrotranslocation complex.
Rao B, Wang Q, Yao D, Xia Y, Li W, Xie Y, Li S, Cao M, Shen Y, Qin A, Zhao J, Cao Y
OpenAccess logo Sci Adv 9 eadi5656 (2023)
PMID: 37831771
Related structures: EMD-33611

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-232467 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Derlin-1 Chains: W, X, Y, Z
Molecule details ›
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
Sequence domains: Der1-like family
Transitional endoplasmic reticulum ATPase Chains: A, B, C, D, E, F
Molecule details ›
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
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 12 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.61Å
Relevant EMDB volumes: EMD-33611
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Biological mechanisms and clinical significance of endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) in human cancer.
Chen et al. (2024)