› 7czb

Electron Microscopy
3.8Å resolution

The cryo-EM structure of the ERAD retrotranslocation channel formed by human Derlin-1

Released:
DOI: 10.2210/pdb7czb/pdb
PDB entry 7czb coloured by chain, front view.
PDB entry 7czb coloured by chain, side view.
PDB entry 7czb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1.
Rao B, Li S, Yao D, Wang Q, Xia Y, Jia Y, Shen Y, Cao Y
Sci Adv 7 (2021)
PMID: 33658201
Related structures: EMD-30508

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Derlin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 251 amino acids
Theoretical weight: 28.82 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9BUN8 (Residues: 1-251; Coverage: 100%)
Gene names: DER1, DERL1, UNQ243/PRO276
Sequence domains: Der1-like family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-30508
Expression system: Homo sapiens

Quick links

Citations

8 review citations

Order through destruction: how ER-associated protein degradation contributes to organelle homeostasis.
Christianson et al. (2022)
7 more

3 mentions without citation

Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates.
Nejatfard et al. (2021)
2 more